SOLUBLE ACETYLCHOLINE RECEPTOR
APLYSIA CALIFORNICA
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count | Chain A； UniProt 20–231 Chain B； UniProt 20–231 Chain C； UniProt 20–231 Chain D； UniProt 20–231 Chain E； UniProt 20–231 | Fragment：SEROTONIN BINDING PROTEIN, UNP RESIDUES 20-231 | QMR VARENICLINE × 5 | X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions | Resolution 2.30 Å R-free 0.224 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
| Other PDB | Difference from Current Entry 5AIN | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 2BR7 Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in complex with HEPES Deposited 2005-05-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Chain B
20–236（217 aa）
Chain C
20–236（217 aa）
Chain D
20–236（217 aa）
Chain E
20–236（217 aa）
|
Not recorded | EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；100 MM HEPES 1.15 M SODIUM MALONATE, pH 7.00
|
Resolution 3.00 Å R-free 0.249 |
| 2BR8 Crystal Structure of Acetylcholine-binding Protein (AChBP) from Aplysia californica in complex with an alpha-conotoxin PnIA variant Deposited 2005-05-03 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
20–236（217 aa）
Chain B
20–236（217 aa）
Chain C
20–236（217 aa）
Chain D
20–236（217 aa）
Chain E
20–236（217 aa）
|
Not recorded | SO4 SULFATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；18 % PEG 3350, 180 MM NA2SO4, 100 MM BIS-TRIS PROPANE PH 7.5
|
Resolution 2.40 Å R-free 0.250 |
| 2BYN Crystal structure of apo AChBP from Aplysia californica Deposited 2005-08-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | PG4 TETRAETHYLENE GLYCOL × 4 1PE PENTAETHYLENE GLYCOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.6；12-14% PEG 4000, 0.1 M SODIUM CITRATE, PH 5.6, 20% ISOPROPANOL, 5% GLYCEROL
|
Resolution 2.02 Å R-free 0.202 |
| 2BYP Crystal structure of Aplysia californica AChBP in complex with alpha- conotoxin ImI Deposited 2005-08-03 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
18–225（208 aa）
Chain B
18–225（208 aa）
Chain C
18–225（208 aa）
Chain D
18–225（208 aa）
Chain E
18–225（208 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；11-14% PEG-4000, 0.1 M TRIS, PH 7.5, 0.4 M MGCL2
|
Resolution 2.07 Å R-free 0.214 |
| 2BYQ Crystal structure of Aplysia californica AChBP in complex with epibatidine Deposited 2005-08-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | EPJ EPIBATIDINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；18-22% PEG-3350, 0.1 M TRIS, PH 7.5, 0.2 M SODIUM CITRATE
|
Resolution 3.40 Å R-free 0.255 |
| 2BYR CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA in complex with methyllycaconitine Deposited 2005-08-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | MLK METHYLLYCACONITINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；22% PEG 4K, 0.1 M TRIS, PH 7.5, 0.4 M MG2CL
|
Resolution 2.45 Å R-free 0.232 |
| 2BYR CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA in complex with methyllycaconitine Deposited 2005-08-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Chain G
18–236（219 aa）
Chain H
18–236（219 aa）
Chain I
18–236（219 aa）
Chain J
18–236（219 aa）
|
Not recorded | MLK METHYLLYCACONITINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；22% PEG 4K, 0.1 M TRIS, PH 7.5, 0.4 M MG2CL
|
Resolution 2.45 Å R-free 0.232 |
| 2BYS CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA IN complex with lobeline Deposited 2005-08-04 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | LOB LOBELINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；25% PEG 4K, 0.1 M HEPES, PH 7.5
|
Resolution 2.05 Å R-free 0.258 |
| 2BYS CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA IN complex with lobeline Deposited 2005-08-04 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Chain G
18–236（219 aa）
Chain H
18–236（219 aa）
Chain I
18–236（219 aa）
Chain J
18–236（219 aa）
|
Not recorded | LOB LOBELINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；25% PEG 4K, 0.1 M HEPES, PH 7.5
|
Resolution 2.05 Å R-free 0.258 |
| 2C9T Crystal Structure Of Acetylcholine Binding Protein (AChBP) From Aplysia Californica In Complex With alpha-Conotoxin ImI Deposited 2005-12-14 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric |
Chain A
20–236（217 aa）
Chain B
20–236（217 aa）
Chain C
20–236（217 aa）
Chain D
20–236（217 aa）
Chain E
20–236（217 aa）
Chain F
20–236（217 aa）
Chain G
20–236（217 aa）
Chain H
20–236（217 aa）
Chain I
20–236（217 aa）
Chain J
20–236（217 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
100 MM SODIUM ACETATE PH 5.5, 12.5% PEG5000 MME
|
Resolution 2.25 Å R-free 0.227 |
| 2PGZ Crystal structure of Cocaine bound to an ACh-Binding Protein Deposited 2007-04-10 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：residues 18-236
Chain B
18–236（219 aa）
Fragment：residues 18-236
Chain C
18–236（219 aa）
Fragment：residues 18-236
Chain D
18–236（219 aa）
Fragment：residues 18-236
Chain E
18–236（219 aa）
Fragment：residues 18-236
|
Not recorded | COC COCAINE × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.1M Tris-HCL 10% (w/v) PEG 400, 15% (w/v) PEG 1000, 2ul drop, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.76 Å R-free 0.210 |
| 2PH9 Galanthamine bound to an ACh-binding Protein Deposited 2007-04-10 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：residues 18-236
Chain B
18–236（219 aa）
Fragment：residues 18-236
Chain C
18–236（219 aa）
Fragment：residues 18-236
Chain D
18–236（219 aa）
Fragment：residues 18-236
Chain E
18–236（219 aa）
Fragment：residues 18-236
|
Not recorded | GNT (-)-GALANTHAMINE × 4 PG4 TETRAETHYLENE GLYCOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；291 K；0.1 M sodium citrate, 10% (w/v) PEG-1000, 24% (v/v) isopropanol, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 2.88 Å R-free 0.237 |
| 2UZ6 AChBP-targeted a-conotoxin correlates distinct binding orientations with nAChR subtype selectivity. Deposited 2007-04-25 | Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.40 Å R-free 0.252 |
| 2UZ6 AChBP-targeted a-conotoxin correlates distinct binding orientations with nAChR subtype selectivity. Deposited 2007-04-25 | Different construct Different oligomeric state Different ligand/ion Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain F
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain G
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain H
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain I
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain J
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 GOL GLYCEROL × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.40 Å R-free 0.252 |
| 2W8F Aplysia californica AChBP bound to in silico compound 31 Deposited 2009-01-16 | Different construct Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | BS1 (3-EXO)-3-(10,11-DIHYDRO-5H-DIBENZO[A,D][7]ANNULEN-5-YLOXY)-8,8-DIMETHYL-8-AZONIABICYCLO[3.2.1]OCTANE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.70 Å R-free 0.267 |
| 2W8F Aplysia californica AChBP bound to in silico compound 31 Deposited 2009-01-16 | Different construct Different ligand/ion Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain G
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain H
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain I
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain J
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | BS1 (3-EXO)-3-(10,11-DIHYDRO-5H-DIBENZO[A,D][7]ANNULEN-5-YLOXY)-8,8-DIMETHYL-8-AZONIABICYCLO[3.2.1]OCTANE × 1 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.70 Å R-free 0.267 |
| 2W8G Aplysia californica AChBP bound to in silico compound 35 Deposited 2009-01-16 | Different construct Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | BS2 (3-ENDO,8-ANTI)-8-BENZYL-3-(10,11-DIHYDRO-5H-DIBENZO[A,D][7]ANNULEN-5-YLOXY)-8-AZONIABICYCLO[3.2.1]OCTANE × 3 | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.60 Å R-free 0.250 |
| 2WN9 Crystal structure of Aplysia ACHBP in complex with 4-0H-DMXBA Deposited 2009-07-07 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | ZY5 4-[(E)-5,6-DIHYDRO-2,3'-BIPYRIDIN-3(4H)-YLIDENEMETHYL]-3-METHOXYPHENOL × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
26% PEG400, 0.1 M HEPES, PH 7.5, 0.2 M MGCL2
|
Resolution 1.75 Å R-free 0.203 |
| 2WNC Crystal structure of Aplysia ACHBP in complex with tropisetron Deposited 2009-07-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | TKT (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-INDOLE-3-CARBOXYLATE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
22% PEG4000, 0.1 M TRIS-HCL PH 7.5, 0.2 M LI2SO4
|
Resolution 2.20 Å R-free 0.212 |
| 2WNJ CRYSTAL STRUCTURE OF APLYSIA ACHBP IN COMPLEX WITH DMXBA Deposited 2009-07-09 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | ZY7 (3E)-3-[(2,4-DIMETHOXYPHENYL)METHYLIDENE]-3,4,5,6-TETRAHYDRO-2,3'-BIPYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
13% PEG4000, 0.1 M HEPES PH 7.5, 15% ISOPROPANOL, 15% GLYCEROL
|
Resolution 1.80 Å R-free 0.206 |
| 2WNL CRYSTAL STRUCTURE OF APLYSIA ACHBP IN COMPLEX WITH ANABASEINE Deposited 2009-07-09 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain G
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain H
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain I
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain J
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | AN4 3,4,5,6-tetrahydro-2,3'-bipyridine × 2 AN5 5-amino-1-pyridin-3-ylpentan-1-one × 2 MG MAGNESIUM ION × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
19% PEG4000, 95 MM NA-CITRATE, PH 5.6, 19% ISOPROPANOL, 5% GLYCEROL
|
Resolution 2.70 Å R-free 0.251 |
| 2WNL CRYSTAL STRUCTURE OF APLYSIA ACHBP IN COMPLEX WITH ANABASEINE Deposited 2009-07-09 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | AN4 3,4,5,6-tetrahydro-2,3'-bipyridine × 3 AN5 5-amino-1-pyridin-3-ylpentan-1-one × 2 PG4 TETRAETHYLENE GLYCOL × 1 MG MAGNESIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
19% PEG4000, 95 MM NA-CITRATE, PH 5.6, 19% ISOPROPANOL, 5% GLYCEROL
|
Resolution 2.70 Å R-free 0.251 |
| 2WZY Crystal structure of A-AChBP in complex with 13-desmethyl spirolide C Deposited 2009-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain G
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain H
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain I
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain J
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | SQX 13-DESMETHYL SPIROLIDE C × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；27-30% PEG-400, 0.1 M HEPES, PH 7.5-7.7, 0.2 M MGCL2
|
Resolution 2.51 Å R-free 0.237 |
| 2WZY Crystal structure of A-AChBP in complex with 13-desmethyl spirolide C Deposited 2009-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | SQX 13-DESMETHYL SPIROLIDE C × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；27-30% PEG-400, 0.1 M HEPES, PH 7.5-7.7, 0.2 M MGCL2
|
Resolution 2.51 Å R-free 0.237 |
| 2X00 CRYSTAL STRUCTURE OF A-ACHBP IN COMPLEX WITH GYMNODIMINE A Deposited 2009-12-04 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain B
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain C
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain D
18–236（219 aa）
Fragment：RESIDUES 18-236
Chain E
18–236（219 aa）
Fragment：RESIDUES 18-236
|
Not recorded | GYN GYMNODIMINE A × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；27-30% PEG-400, 0.1 M HEPES, PH 7.5-7.7, 0.2 M MGCL2
|
Resolution 2.40 Å R-free 0.235 |
| 2XNT Acetylcholine binding protein (AChBP) as template for hierarchical in silico screening procedures to identify structurally novel ligands for the nicotinic receptors Deposited 2010-08-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | VU2 (2S)-2-[(4-CHLOROBENZYL)OXY]-2-PHENYLETHANAMINE × 5 BR BROMIDE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；0.2M SODIUM BROMIDE, 0.1M BIS-TRIS PROPANE PH 7.5, 20% PEG 1000
|
Resolution 3.21 Å R-free 0.232 |
| 2XNT Acetylcholine binding protein (AChBP) as template for hierarchical in silico screening procedures to identify structurally novel ligands for the nicotinic receptors Deposited 2010-08-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | VU2 (2S)-2-[(4-CHLOROBENZYL)OXY]-2-PHENYLETHANAMINE × 5 BR BROMIDE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；0.2M SODIUM BROMIDE, 0.1M BIS-TRIS PROPANE PH 7.5, 20% PEG 1000
|
Resolution 3.21 Å R-free 0.232 |
| 2XNU Acetylcholine binding protein (AChBP) as template for hierarchical in silico screening procedures to identify structurally novel ligands for the nicotinic receptors Deposited 2010-08-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | VU3 2-(2-(4-PHENYLPIPERIDIN-1-YL)ETHYL)-1H-INDOLE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；0.2M SODIUM BROMIDE, 0.1M BIS-TRIS PROPANE PH 7.5, 20% PEG3350
|
Resolution 2.55 Å R-free 0.230 |
| 2XNV Acetylcholine binding protein (AChBP) as template for hierarchical in silico screening procedures to identify structurally novel ligands for the nicotinic receptors Deposited 2010-08-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | VU3 2-(2-(4-PHENYLPIPERIDIN-1-YL)ETHYL)-1H-INDOLE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2M SODIUM FORMATE, pH 7
|
Resolution 2.44 Å R-free 0.212 |
| 2XNV Acetylcholine binding protein (AChBP) as template for hierarchical in silico screening procedures to identify structurally novel ligands for the nicotinic receptors Deposited 2010-08-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | VU3 2-(2-(4-PHENYLPIPERIDIN-1-YL)ETHYL)-1H-INDOLE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；2M SODIUM FORMATE, pH 7
|
Resolution 2.44 Å R-free 0.212 |
| 2XYS Crystal structure of Aplysia californica AChBP in complex with strychnine Deposited 2010-11-19 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | SY9 STRYCHNINE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM SODIUM ACETATE, 100 MM BISTRISPROPANE AT PH 8.5, 15.5% PEG3350
|
Resolution 1.91 Å R-free 0.210 |
| 2XYT Crystal structure of Aplysia californica AChBP in complex with d- tubocurarine Deposited 2010-11-19 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | TC9 D-TUBOCURARINE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM NA2 SO4, 100 MM BISTRISPROPANE PH 8.5, 15% PEG 3350.
|
Resolution 2.05 Å R-free 0.220 |
| 2XYT Crystal structure of Aplysia californica AChBP in complex with d- tubocurarine Deposited 2010-11-19 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain G
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain H
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain I
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain J
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | TC9 D-TUBOCURARINE × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM NA2 SO4, 100 MM BISTRISPROPANE PH 8.5, 15% PEG 3350.
|
Resolution 2.05 Å R-free 0.220 |
| 2XZ5 MMTS-modified Y53C mutant of Aplysia AChBP in complex with acetylcholine Deposited 2010-11-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | ACH ACETYLCHOLINE × 10 CL CHLORIDE ION × 5 PO4 PHOSPHATE ION × 10 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 7 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM NH4(H2PO4), 100 MM TRIS PH 8.5 AND 50% MPD.
|
Resolution 2.80 Å R-free 0.219 |
| 2XZ6 MTSET-modified Y53C mutant of Aplysia AChBP Deposited 2010-11-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain G
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain H
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain I
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain J
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | ETM 2-(TRIMETHYLAMMONIUM)ETHYL THIOL × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
150 MM KSCN, BISTRISPROPANE PH 8.5, 14% PEG 3350.
|
Resolution 3.14 Å R-free 0.236 |
| 2XZ6 MTSET-modified Y53C mutant of Aplysia AChBP Deposited 2010-11-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | ETM 2-(TRIMETHYLAMMONIUM)ETHYL THIOL × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
150 MM KSCN, BISTRISPROPANE PH 8.5, 14% PEG 3350.
|
Resolution 3.14 Å R-free 0.236 |
| 2Y54 Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Fragment 1) Deposited 2011-01-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | V63 [(1R,5S)-8-AZABICYCLO[3.2.1]OCTAN-3-YL] BENZOATE × 5 SO4 SULFATE ION × 2 CL CHLORIDE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.5；0.1M MMT PH7.5, 0.9M AMMONIUM SULPHATE
|
Resolution 3.65 Å R-free 0.217 |
| 2Y56 Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 3) Deposited 2011-01-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | V11 [(1S,5R)-8-[(2R)-2-HYDROXY-2-PHENYL-ETHYL]-8-AZABICYCLO[3.2.1]OCTAN-3-YL] BENZOATE × 5 CL CHLORIDE ION × 12 SO4 SULFATE ION × 14 GOL GLYCEROL × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8.5；0.1M MMT PH8.5, 1.1M AMMONIUM SULPHATE
|
Resolution 3.59 Å R-free 0.203 |
| 2Y57 Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 4) Deposited 2011-01-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | V37 [(1R,5S)-8-PHENETHYL-8-AZABICYCLO[3.2.1]OCTAN-3-YL] BENZOATE × 5 CL CHLORIDE ION × 5 SO4 SULFATE ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；0.1M MMT PH8.0, 1.3M AMMONIUM SULPHATE
|
Resolution 3.30 Å R-free 0.193 |
| 2Y58 Fragment growing induces conformational changes in acetylcholine- binding protein: A structural and thermodynamic analysis - (Compound 6) Deposited 2011-01-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | V38 [(1R,5S)-8-[(2R)-2-HYDROXY-2-PHENYL-ETHYL]-8-METHYL-8-AZONIABICYCLO[3.2.1]OCTAN-3-YL] BENZOATE × 5 CL CHLORIDE ION × 6 SO4 SULFATE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；0.1M MMT PH 7.0, 1.4M AMMONIUM SULPHATE
|
Resolution 3.25 Å R-free 0.198 |
| 2Y7Y APLYSIA CALIFORNICA ACHBP IN APO STATE Deposited 2011-02-02 | Different construct Different ligand/ion Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 1.90 Å R-free 0.227 |
| 2YMD Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with serotonin (5-hydroxytryptamine) Deposited 2012-10-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric |
Chain A
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain B
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain C
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain D
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain E
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain F
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain G
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain H
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain I
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain J
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | SRO SEROTONIN × 10 GOL GLYCEROL × 14 PO4 PHOSPHATE ION × 10 |
X-RAY DIFFRACTION
X-ray crystallization conditions
400 MM (NH4)H2PO4
|
Resolution 1.96 Å R-free 0.201 |
| 2YMD Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with serotonin (5-hydroxytryptamine) Deposited 2012-10-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain B
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain C
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain D
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain E
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | SRO SEROTONIN × 5 GOL GLYCEROL × 9 PO4 PHOSPHATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
400 MM (NH4)H2PO4
|
Resolution 1.96 Å R-free 0.201 |
| 2YMD Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with serotonin (5-hydroxytryptamine) Deposited 2012-10-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain G
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain H
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain I
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
Chain J
20–231（212 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-231
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | SRO SEROTONIN × 5 GOL GLYCEROL × 5 PO4 PHOSPHATE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
400 MM (NH4)H2PO4
|
Resolution 1.96 Å R-free 0.201 |
| 2YME Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with granisetron Deposited 2012-10-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain G
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain H
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain I
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain J
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 CWB 1-methyl-N-[(1R,5S)-9-methyl-9-azabicyclo[3.3.1]nonan-3-yl]indazole-3-carboxamide × 5 PO4 PHOSPHATE ION × 2 NA SODIUM ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM NA2SO4, BISTRISPROPANE PH 8.5, 18% PEG3350.
|
Resolution 2.40 Å R-free 0.226 |
| 2YME Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with granisetron Deposited 2012-10-09 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain B
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain C
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain D
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
Chain E
20–224（205 aa）
Fragment：ACETYLCHOLINE BINDING DOMAIN, RESIDUES 20-224
|
Mutation：YES Mutation：YES Mutation：YES Mutation：YES Mutation：YES | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 CWB 1-methyl-N-[(1R,5S)-9-methyl-9-azabicyclo[3.3.1]nonan-3-yl]indazole-3-carboxamide × 5 PO4 PHOSPHATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
200 MM NA2SO4, BISTRISPROPANE PH 8.5, 18% PEG3350.
|
Resolution 2.40 Å R-free 0.226 |
| 3C79 Crystal structure of Aplysia californica AChBP in complex with the neonicotinoid imidacloprid Deposited 2008-02-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | IM4 (2E)-1-[(6-chloropyridin-3-yl)methyl]-N-nitroimidazolidin-2-imine × 4 IPA ISOPROPYL ALCOHOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；22% isopropanol, 0.2M magnesium chloride, 0.1 M Hepes pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 2.48 Å R-free 0.250 |
| 3C84 Crystal structure of a complex of AChBP from aplysia californica and the neonicotinoid thiacloprid Deposited 2008-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | TH4 {(2Z)-3-[(6-chloropyridin-3-yl)methyl]-1,3-thiazolidin-2-ylidene}cyanamide × 4 IPA ISOPROPYL ALCOHOL × 7 MG MAGNESIUM ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；30% isopropanol, 0.2M magnesium chloride, 0.1M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
|
Resolution 1.94 Å R-free 0.215 |
| 3GUA Sulfates bound in the vestibule of AChBP Deposited 2009-03-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain B
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain C
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain D
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain E
18–225（208 aa）
Fragment：sequence database residues 18-225
|
Not recorded | SO4 SULFATE ION × 12 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；.1 ul protein (10mg/ml tris buffered saline) and .1ul reservoir solution (1.26M ammonium sulfate, and 0.1M cacodylate), pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
|
Resolution 3.10 Å R-free 0.250 |
| 3GUA Sulfates bound in the vestibule of AChBP Deposited 2009-03-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain G
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain H
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain I
18–225（208 aa）
Fragment：sequence database residues 18-225
Chain J
18–225（208 aa）
Fragment：sequence database residues 18-225
|
Not recorded | SO4 SULFATE ION × 9 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；.1 ul protein (10mg/ml tris buffered saline) and .1ul reservoir solution (1.26M ammonium sulfate, and 0.1M cacodylate), pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
|
Resolution 3.10 Å R-free 0.250 |
| 3PEO Crystal structure of acetylcholine binding protein complexed with metocurine Deposited 2010-10-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | CU9 6,6',7',12'-tetramethoxy-2,2,2',2'-tetramethyltubocuraran-2,2'-diium × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；10% PEG 4000, 0.25M magnesium chloride, 0.1M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 2.10 Å R-free 0.255 |
| 3PEO Crystal structure of acetylcholine binding protein complexed with metocurine Deposited 2010-10-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Chain G
18–236（219 aa）
Chain H
18–236（219 aa）
Chain I
18–236（219 aa）
Chain J
18–236（219 aa）
|
Not recorded | CU9 6,6',7',12'-tetramethoxy-2,2,2',2'-tetramethyltubocuraran-2,2'-diium × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；10% PEG 4000, 0.25M magnesium chloride, 0.1M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 2.10 Å R-free 0.255 |
| 3PMZ Crystal Structure of the Complex of Acetylcholine Binding Protein and d-tubocurarine Deposited 2010-11-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain B
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain C
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain D
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain E
18–236（219 aa）
Fragment：UNP Residues 18-228
|
Not recorded | MG MAGNESIUM ION × 10 TUB (1beta,1'alpha)-7',12'-dihydroxy-6,6'-dimethoxy-2,2',2'-trimethyltubocuraran-2'-ium × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；295 K；10% PEG 4000, 0.25M magnesium chloride, 0.1M Tris buffer pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 2.44 Å R-free 0.294 |
| 3PMZ Crystal Structure of the Complex of Acetylcholine Binding Protein and d-tubocurarine Deposited 2010-11-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain G
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain H
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain I
18–236（219 aa）
Fragment：UNP Residues 18-228
Chain J
18–236（219 aa）
Fragment：UNP Residues 18-228
|
Not recorded | MG MAGNESIUM ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；295 K；10% PEG 4000, 0.25M magnesium chloride, 0.1M Tris buffer pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K
|
Resolution 2.44 Å R-free 0.294 |
| 3SH1 Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR Deposited 2011-06-15 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：unp entry 18-236
Chain B
18–236（219 aa）
Fragment：unp entry 18-236
Chain C
18–236（219 aa）
Fragment：unp entry 18-236
Chain D
18–236（219 aa）
Fragment：unp entry 18-236
Chain E
18–236（219 aa）
Fragment：unp entry 18-236
|
Not recorded | MG MAGNESIUM ION × 4 MLK METHYLLYCACONITINE × 5 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；30%MPD, 0.1M Na Cacodylate, 0.2M Magnesium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 2.90 Å R-free 0.258 |
| 3SH1 Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR Deposited 2011-06-15 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：unp entry 18-236
Chain G
18–236（219 aa）
Fragment：unp entry 18-236
Chain H
18–236（219 aa）
Fragment：unp entry 18-236
Chain I
18–236（219 aa）
Fragment：unp entry 18-236
Chain J
18–236（219 aa）
Fragment：unp entry 18-236
|
Not recorded | MG MAGNESIUM ION × 1 MLK METHYLLYCACONITINE × 5 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；290 K；30%MPD, 0.1M Na Cacodylate, 0.2M Magnesium Acetate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 2.90 Å R-free 0.258 |
| 3SIO Ac-AChBP ligand binding domain (not including beta 9-10 linker) mutated to human alpha-7 nAChR Deposited 2011-06-19 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：unp entry 18-236
Chain B
18–236（219 aa）
Fragment：unp entry 18-236
Chain C
18–236（219 aa）
Fragment：unp entry 18-236
Chain D
18–236（219 aa）
Fragment：unp entry 18-236
Chain E
18–236（219 aa）
Fragment：unp entry 18-236
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 MLK METHYLLYCACONITINE × 5 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.6；298 K；0.1M Sodium Acetate, 0.02M Calcium Chloride, 30% 2-Methyl-2,4-Pentanediol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.32 Å R-free 0.230 |
| 3SIO Ac-AChBP ligand binding domain (not including beta 9-10 linker) mutated to human alpha-7 nAChR Deposited 2011-06-19 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：unp entry 18-236
Chain G
18–236（219 aa）
Fragment：unp entry 18-236
Chain H
18–236（219 aa）
Fragment：unp entry 18-236
Chain I
18–236（219 aa）
Fragment：unp entry 18-236
Chain J
18–236（219 aa）
Fragment：unp entry 18-236
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 MLK METHYLLYCACONITINE × 5 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 3 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 4.6；298 K；0.1M Sodium Acetate, 0.02M Calcium Chloride, 30% 2-Methyl-2,4-Pentanediol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.32 Å R-free 0.230 |
| 3T4M Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR (intermediate) Deposited 2011-07-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：unp residues 18-236
Chain B
18–236（219 aa）
Fragment：unp residues 18-236
Chain C
18–236（219 aa）
Fragment：unp residues 18-236
Chain D
18–236（219 aa）
Fragment：unp residues 18-236
Chain E
18–236（219 aa）
Fragment：unp residues 18-236
|
Not recorded | CA CALCIUM ION × 5 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；0.1M sodium acetate, 0.02M calcium chloride, 30% 2-methyl-2,4-pentanediol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 3.00 Å R-free 0.240 |
| 3T4M Ac-AChBP ligand binding domain mutated to human alpha-7 nAChR (intermediate) Deposited 2011-07-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：unp residues 18-236
Chain G
18–236（219 aa）
Fragment：unp residues 18-236
Chain H
18–236（219 aa）
Fragment：unp residues 18-236
Chain I
18–236（219 aa）
Fragment：unp residues 18-236
Chain J
18–236（219 aa）
Fragment：unp residues 18-236
|
Not recorded | CA CALCIUM ION × 4 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 5 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；290 K；0.1M sodium acetate, 0.02M calcium chloride, 30% 2-methyl-2,4-pentanediol, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K
|
Resolution 3.00 Å R-free 0.240 |
| 4AFT Aplysia californica AChBP in complex with Varenicline Deposited 2012-01-23 | Different construct Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | QMR VARENICLINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；0.6-1.2 M AMMONIUM SULPHATE, 0.1 M MMT PH 6.5-8.5
|
Resolution 3.20 Å R-free 0.213 |
| 4BFQ Assembly of a triple pi-stack of ligands in the binding site of Aplysia californica acetylcholine binding protein (AChBP) Deposited 2013-03-21 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Chain B
20–236（217 aa）
Chain C
20–236（217 aa）
Chain D
20–236（217 aa）
Chain E
20–236（217 aa）
|
Not recorded | 083 4,6-dimethyl-N'-(3-pyridin-2-ylisoquinolin-1-yl)pyrimidine-2-carboximidamide × 14 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION；pH 8；292 K；THE VUF9432-AC-ACHBP COMPLEX WAS FORMED BY MIXING THE PROTEIN AT 3.5 MG/ML WITH 1MM VUF9432 AND INCUBATING ON ICE FOR 1 HOUR. CRYSTALS WERE GROWN USING THE VAPOUR DIFFUSION METHOD IN A SOLUTION CONSISTING OF 0.2M LISO4, 0.8M AMMONIUM SULPHATE IN MMT BUFFER (PH 8.0) AND 19 DEGREES C
|
Resolution 2.40 Å R-free 0.247 |
| 4BQT Aplysia californica AChBP in complex with Cytisine Deposited 2013-06-02 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain B
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain C
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain D
20–236（217 aa）
Fragment：RESIDUES 20-236
Chain E
20–236（217 aa）
Fragment：RESIDUES 20-236
|
Not recorded | C5E (1R,5S)-1,2,3,4,5,6-HEXAHYDRO-8H-1,5-METHANOPYRIDO[1,2-A][1,5]DIAZOCIN-8-ONE × 5 CL CHLORIDE ION × 11 CO COBALT (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7；0.6-1.2 M AMMONIUM SULPHATE, 0.1 M MMT PH 6.5-8.5
|
Resolution 2.88 Å R-free 0.224 |
| 4DBM Aplysia californica-AChBP in complex with triazole 18 Deposited 2012-01-16 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 0J0 (3-exo)-8,8-dimethyl-3-(4-{[(1-methyl-2-oxo-1,2-dihydroquinolin-4-yl)oxy]methyl}-1H-1,2,3-triazol-1-yl)-8-azoniabicyclo[3.2.1]octane × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 8；295 K；0.1M Tris-HCl, 0.25M magnesium chloride, 12% (w/v) PEG 4000, 10% (v/v) glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.30 Å R-free 0.252 |
| 4EZ1 Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with alpha-conotoxin BuIA Deposited 2012-05-02 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Not recorded | MN MANGANESE (II) ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M Tris-HCl, 0.25 M magnesium chloride, 20% w/v PEG4000, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|
Resolution 2.49 Å R-free 0.227 |
| 4FRR X-ray structure of Acetylcholine binding protein from Aplysia californica in presence of 3-((S)-azetidin-2-ylmethoxy)-5-((1S,2R)-2-(2-methoxyethyl)cyclopropyl)pyridine Deposited 2012-06-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：UNP residues 18-225
Chain B
18–225（208 aa）
Fragment：UNP residues 18-225
Chain C
18–225（208 aa）
Fragment：UNP residues 18-225
Chain D
18–225（208 aa）
Fragment：UNP residues 18-225
Chain E
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | 0VC 3-[(2S)-azetidin-2-ylmethoxy]-5-[(1S,2R)-2-(2-methoxyethyl)cyclopropyl]pyridine × 3 GOL GLYCEROL × 15 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Tris HCl,7.5, 15% PEG 4000 and 0.2M MgCl2 . , VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.20 Å R-free 0.246 |
| 4FRR X-ray structure of Acetylcholine binding protein from Aplysia californica in presence of 3-((S)-azetidin-2-ylmethoxy)-5-((1S,2R)-2-(2-methoxyethyl)cyclopropyl)pyridine Deposited 2012-06-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–225（208 aa）
Fragment：UNP residues 18-225
Chain G
18–225（208 aa）
Fragment：UNP residues 18-225
Chain H
18–225（208 aa）
Fragment：UNP residues 18-225
Chain I
18–225（208 aa）
Fragment：UNP residues 18-225
Chain J
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | 0VC 3-[(2S)-azetidin-2-ylmethoxy]-5-[(1S,2R)-2-(2-methoxyethyl)cyclopropyl]pyridine × 3 GOL GLYCEROL × 11 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.1M Tris HCl,7.5, 15% PEG 4000 and 0.2M MgCl2 . , VAPOR DIFFUSION, HANGING DROP, temperature 293K
|
Resolution 2.20 Å R-free 0.246 |
| 4WV9 Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with click chemistry compound (3-exo)-8,8-dimethyl-3-[4-(pyridin-4-yl)-1H-1,2,3-triazol-1-yl]-8-azoniabicyclo[3.2.1]octane Deposited 2014-11-04 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–224（207 aa）
Fragment：UNP residues 18-224
Chain B
18–224（207 aa）
Fragment：UNP residues 18-224
Chain C
18–224（207 aa）
Fragment：UNP residues 18-224
Chain D
18–224（207 aa）
Fragment：UNP residues 18-224
Chain E
18–224（207 aa）
Fragment：UNP residues 18-224
|
Not recorded | MD4 (3-exo)-8,8-dimethyl-3-[4-(pyridin-4-yl)-1H-1,2,3-triazol-1-yl]-8-azoniabicyclo[3.2.1]octane × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.6；297 K；0.1 M Sodium citrate tribasic dihydrate, pH 5.6, 20% v/v 2-Propanol, 20% w/v Polyethylene glycol 4000
|
Resolution 2.00 Å R-free 0.220 |
| 4XHE Crystal Structure of A-AChBP in complex with pinnatoxin A Deposited 2015-01-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：UNP residues 18-225
Chain B
18–225（208 aa）
Fragment：UNP residues 18-225
Chain C
18–225（208 aa）
Fragment：UNP residues 18-225
Chain D
18–225（208 aa）
Fragment：UNP residues 18-225
Chain E
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | 40P Pinnatoxin A × 5 CA CALCIUM ION × 2 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；18% (w/v) P400, 0.1M Hepes pH 7.5, 0.2M CaCl2, 5% glycerol
|
Resolution 1.90 Å R-free 0.216 |
| 4XHE Crystal Structure of A-AChBP in complex with pinnatoxin A Deposited 2015-01-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–225（208 aa）
Fragment：UNP residues 18-225
Chain G
18–225（208 aa）
Fragment：UNP residues 18-225
Chain H
18–225（208 aa）
Fragment：UNP residues 18-225
Chain I
18–225（208 aa）
Fragment：UNP residues 18-225
Chain J
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | 40P Pinnatoxin A × 5 CA CALCIUM ION × 1 CL CHLORIDE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；18% (w/v) P400, 0.1M Hepes pH 7.5, 0.2M CaCl2, 5% glycerol
|
Resolution 1.90 Å R-free 0.216 |
| 4XK9 Crystal structure of A-AChBP in complex with pinnatoxin G Deposited 2015-01-10 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Not recorded | 41J Pinnatoxin G × 5 CL CHLORIDE ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；8% (w/v) P4000, 0.1M Hepes pH 7.5, 0.2M MgCl2
|
Resolution 2.20 Å R-free 0.211 |
| 4XK9 Crystal structure of A-AChBP in complex with pinnatoxin G Deposited 2015-01-10 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：UNP residues 18-236
Chain G
18–236（219 aa）
Fragment：UNP residues 18-236
Chain H
18–236（219 aa）
Fragment：UNP residues 18-236
Chain I
18–236（219 aa）
Fragment：UNP residues 18-236
Chain J
18–236（219 aa）
Fragment：UNP residues 18-236
|
Not recorded | 41J Pinnatoxin G × 5 CL CHLORIDE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；8% (w/v) P4000, 0.1M Hepes pH 7.5, 0.2M MgCl2
|
Resolution 2.20 Å R-free 0.211 |
| 4ZJS Crystal structure of a chimeric acetylcholine binding protein from Aplysia Californica (Ac-AChBP) containing the main immunogenic region (MIR) from the human alpha 1 subunit of the muscle nicotinic acetylcholine receptor in complex with anatoxin-A. Deposited 2015-04-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
48–77（30 aa）
Chain A
99–236（138 aa）
Chain B
48–77（30 aa）
Chain B
99–236（138 aa）
Chain C
48–77（30 aa）
Chain C
99–236（138 aa）
Chain D
48–77（30 aa）
Chain D
99–236（138 aa）
Chain E
48–77（30 aa）
Chain E
99–236（138 aa）
|
Not recorded | 4P0 1-[(1R,6R)-9-azabicyclo[4.2.1]non-2-en-2-yl]ethanone × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；297 K；17. 25.5% PEG 4000, 0.085 M Tris HCl pH 8.5, 0.17 M Lithium Sulfate, 15% Glycerol
|
Resolution 2.23 Å R-free 0.228 |
| 4ZK4 Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with 7-(5-isopropoxy-pyridin-3-yl)-1-methyl-1,7-diaza-spiro[4.4]nonane Deposited 2015-04-29 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain A
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
|
Not recorded | MG MAGNESIUM ION × 2 SO4 SULFATE ION × 5 PG4 TETRAETHYLENE GLYCOL × 1 TII (5R)-1-methyl-7-[5-(propan-2-yloxy)pyridin-3-yl]-1,7-diazaspiro[4.4]nonane × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；298 K；1.7% PEG400, 0.085 M HEPES sodium, pH 7.5, 1.7 M ammonium sulfate, 15% glycerol
|
Resolution 1.90 Å R-free 0.212 |
| 5BRX X-ray crystal structure of Aplysia californica (Ac-AChBP) in complex with 2-pyridyl azatricyclo[3.3.1.13,7]decane; 2-pyridylazaadamantane; 2-Aza (TI-8480) Deposited 2015-06-01 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W | SO4 SULFATE ION × 5 TI4 (2R,3S,5R,7S)-2-(pyridin-3-yl)-1-azatricyclo[3.3.1.1~3,7~]decane × 2 PG4 TETRAETHYLENE GLYCOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 2.05 Å R-free 0.235 |
| 5BRX X-ray crystal structure of Aplysia californica (Ac-AChBP) in complex with 2-pyridyl azatricyclo[3.3.1.13,7]decane; 2-pyridylazaadamantane; 2-Aza (TI-8480) Deposited 2015-06-01 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
18–236（219 aa）
Fragment：UNP residues 18-236
Chain G
18–236（219 aa）
Fragment：UNP residues 18-236
Chain H
18–236（219 aa）
Fragment：UNP residues 18-236
Chain I
18–236（219 aa）
Fragment：UNP residues 18-236
Chain J
18–236（219 aa）
Fragment：UNP residues 18-236
|
Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W | SO4 SULFATE ION × 5 TI4 (2R,3S,5R,7S)-2-(pyridin-3-yl)-1-azatricyclo[3.3.1.1~3,7~]decane × 2 PG4 TETRAETHYLENE GLYCOL × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 2.05 Å R-free 0.235 |
| 5BW2 X-ray crystal structure of Aplysia californica acetylcholine binding protein (Ac-AChBP) Y55W in complex with 2-Pyridin-3-yl-1-aza-bicyclo[2.2.2]octane; 2-(3-pyridyl)quinuclidine; 2-PQ (TI-4699) Deposited 2015-06-05 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W Mutation：Y55W | 4VU (2R)-2-(pyridin-3-yl)-1-azabicyclo[2.2.2]octane × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 2.27 Å R-free 0.222 |
| 5CO5 Crystal structure of Ac-AChBP in complex with conotoxin GIC Deposited 2015-07-19 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain D
1–236（236 aa）
Chain G
1–236（236 aa）
Chain I
1–236（236 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；291 K；1.5M lithium sulfate monohydrate, 0.1M Tris pH 8.5
|
Resolution 2.10 Å R-free 0.221 |
| 5JME Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with alpha-conotoxin PeIA Deposited 2016-04-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；290 K；0.1 M Tris-HCl, 0.25 M magnesium chloride, 20% w/v PEG4000
|
Resolution 2.34 Å R-free 0.229 |
| 5KE4 Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 6 nicotinic acetylcholine receptor in complex with 2-((5-(3,7-Diazabicyclo[3.3.1]nonan-3-yl)pyridin-3-yl)oxy)- N,N-dimethylethanamine (BPC) Deposited 2016-06-09 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 18-236
Chain B
18–236（219 aa）
Fragment：UNP residues 18-236
Chain C
18–236（219 aa）
Fragment：UNP residues 18-236
Chain D
18–236（219 aa）
Fragment：UNP residues 18-236
Chain E
18–236（219 aa）
Fragment：UNP residues 18-236
|
Not recorded | 6S7 2-((5-(3,7-Diazabicyclo[3.3.1]nonan-3-yl)pyridin-3-yl)oxy)-N,N-dimethylethanamine × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；30% PEG 400, 0.1 M HEPES - Na pH 7.5, 0.2 M Magnesium Chloride
|
Resolution 2.55 Å R-free 0.235 |
| 5KZU Crystal structure of an acetylcholine binding protein from Aplysia californica (Ac-AChBP) in complex with click chemistry compound 9-[[1-[8-methyl-8-(2-phenylethyl)-8-azoniabicyclo[3.2.1]octan-3-yl]triazol-4-yl]methyl]carbazole Deposited 2016-07-25 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Fragment：UNP residues 16-236
Chain B
18–236（219 aa）
Fragment：UNP residues 16-236
Chain C
18–236（219 aa）
Fragment：UNP residues 16-236
Chain D
18–236（219 aa）
Fragment：UNP residues 16-236
Chain E
18–236（219 aa）
Fragment：UNP residues 16-236
|
Not recorded | SO4 SULFATE ION × 5 PG4 TETRAETHYLENE GLYCOL × 2 74S 9-[[1-[8-methyl-8-(2-phenylethyl)-8-azoniabicyclo[3.2.1]octan-3-yl]triazol-4-yl]methyl]carbazole × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；290 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 2.30 Å R-free 0.229 |
| 5LXB Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with palonosetron Deposited 2016-09-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 7A9 palonosetron × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；200 mM sodium 265 citrate, 100 mM bis tris propane pH 8.5, and 20% (w/v) PEG3350.
|
Resolution 2.34 Å R-free 0.245 |
| 5LXB Crystal structure of a mutant binding protein (5HTBP-AChBP) in complex with palonosetron Deposited 2016-09-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 7A9 palonosetron × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；200 mM sodium 265 citrate, 100 mM bis tris propane pH 8.5, and 20% (w/v) PEG3350.
|
Resolution 2.34 Å R-free 0.245 |
| 5O87 Crystal structure of wild type Aplysia californica AChBP in complex with nicotine Deposited 2017-06-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 EDO 1,2-ETHANEDIOL × 22 PO4 PHOSPHATE ION × 10 IPA ISOPROPYL ALCOHOL × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.45 M ammonium phosphate monobasic
2 % glycerol
2 % IPA
|
Resolution 2.20 Å R-free 0.235 |
| 5O87 Crystal structure of wild type Aplysia californica AChBP in complex with nicotine Deposited 2017-06-12 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | NCT (S)-3-(1-METHYLPYRROLIDIN-2-YL)PYRIDINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 EDO 1,2-ETHANEDIOL × 20 PO4 PHOSPHATE ION × 10 IPA ISOPROPYL ALCOHOL × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；0.45 M ammonium phosphate monobasic
2 % glycerol
2 % IPA
|
Resolution 2.20 Å R-free 0.235 |
| 5O8T Crystal structure of wild type Aplysia californica AChBP in complex with strychnine Deposited 2017-06-14 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | SY9 STRYCHNINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Reservoir contained 0.1 M magnesium chloride, 25% PEG 3350. Protein buffer 50 mm tris, 250 mM NaCl, pH 7.5. 0.5 mM strychnine
|
Resolution 2.20 Å R-free 0.229 |
| 5OA0 Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, W164F) Deposited 2017-06-20 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, W164F Mutation：T53F, Q74R, Y110A, I135S, W164F Mutation：T53F, Q74R, Y110A, I135S, W164F Mutation：T53F, Q74R, Y110A, I135S, W164F Mutation：T53F, Q74R, Y110A, I135S, W164F | SY9 STRYCHNINE × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 12 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Rservoir contained .0.1 M MgCl2, 25% PEG 3350. Protein buffer 50 mM tris, 250 mM NaCl, 0.5 mM strychnine. Cryo 30 % glycerol
|
Resolution 2.60 Å R-free 0.227 |
| 5OAD Crystal structure of mutant AChBP in complex with HEPES (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-21 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 3 EDO 1,2-ETHANEDIOL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；reservoir condition: 0.1 M HEPES pH 8, 25% PEG 2k MME
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 5mM tropisetron
|
Resolution 2.10 Å R-free 0.255 |
| 5OAJ Crystal structure of mutant AChBP in complex with tropisetron (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 20 FLC CITRATE ANION × 1 TKT (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-INDOLE-3-CARBOXYLATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Reservoir condition: 20% PEG3350, 0.2 M Na citrate.
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 5 mM tropisetron
|
Resolution 2.47 Å R-free 0.208 |
| 5OAJ Crystal structure of mutant AChBP in complex with tropisetron (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 EDO 1,2-ETHANEDIOL × 22 FLC CITRATE ANION × 2 TKT (3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL 1H-INDOLE-3-CARBOXYLATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Reservoir condition: 20% PEG3350, 0.2 M Na citrate.
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 5 mM tropisetron
|
Resolution 2.47 Å R-free 0.208 |
| 5OAL Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | SY9 STRYCHNINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Reservoir buffer: 20 % PEG3350
0.2 M Mg formate
Protein buffer: 50 mM trism 250 mM NaCl Ph 7.5, 0.5 mM strychnine
|
Resolution 3.20 Å R-free 0.231 |
| 5OAL Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | SY9 STRYCHNINE × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Reservoir buffer: 20 % PEG3350
0.2 M Mg formate
Protein buffer: 50 mM trism 250 mM NaCl Ph 7.5, 0.5 mM strychnine
|
Resolution 3.20 Å R-free 0.231 |
| 5OAL Crystal structure of mutant AChBP in complex with strychnine (T53F, Q74R, Y110A, I135S, G162E) Deposited 2017-06-22 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain K
1–236（236 aa）
Chain L
1–236（236 aa）
Chain M
1–236（236 aa）
Chain N
1–236（236 aa）
Chain O
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E Mutation：T53F, Q74R, Y110A, I135S, G162E | SY9 STRYCHNINE × 5 ARG ARGININE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；Reservoir buffer: 20 % PEG3350
0.2 M Mg formate
Protein buffer: 50 mM trism 250 mM NaCl Ph 7.5, 0.5 mM strychnine
|
Resolution 3.20 Å R-free 0.231 |
| 5OAN Crystal structure of mutant AChBP in complex with glycine (T53F, Q74R, Y110A, I135S, G162E, S206CCP_KGTG) Deposited 2017-06-23 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G | CL CHLORIDE ION × 5 ACT ACETATE ION × 5 GLY GLYCINE × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 4.6；293 K；Reservoir solution:2 M sodium formate, 0.1 M sodium acetate pH 4.6 .
Protein buffer: 50 mM tris, 250 mM NaCl, 0.1 M glycine
|
Resolution 2.60 Å R-free 0.235 |
| 5OBG Crystal structure of glycine binding protein in complex with strychnine Deposited 2017-06-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | SY9 STRYCHNINE × 5 EDO 1,2-ETHANEDIOL × 31 NA SODIUM ION × 5 ACT ACETATE ION × 9 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Reservoir buffer: 20 % PEG 3350, 0.2 M MgOAc
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 0.5 mM strychnine
|
Resolution 2.00 Å R-free 0.250 |
| 5OBH Crystal structure of glycine binding protein in complex with bicuculline Deposited 2017-06-27 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G Mutation：T53F, Q74R, Y110A, I135S, G162E, S206K, C207G, C208T, P209G | J94 (5S)-6,6-dimethyl-5-[(6R)-8-oxo-6,8-dihydrofuro[3,4-e][1,3]benzodioxol-6-yl]-5,6,7,8-tetrahydro[1,3]dioxolo[4,5-g]isoquinolin-6-ium × 5 CL CHLORIDE ION × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；Reservoir buffer: 0.2 M ammonium formate, 20 % PEG 3350
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5. 2 mM bicuculline
|
Resolution 2.40 Å R-free 0.249 |
| 5SYO Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with Cytisine Deposited 2016-08-11 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain A
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
|
Not recorded | C5E (1R,5S)-1,2,3,4,5,6-HEXAHYDRO-8H-1,5-METHANOPYRIDO[1,2-A][1,5]DIAZOCIN-8-ONE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；291 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 2.00 Å R-free 0.227 |
| 5TSF Crystal structure of AChBP from Aplysia californica complex with 2-aminopyrimidine at pH 7.0 spacegroup P212121 Deposited 2016-10-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | 7KO 6-chloro-N~4~,N~4~-bis[(pyridin-3-yl)methyl]pyrimidine-2,4-diamine × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；281 K；20% PEG 4000, 0.1M HEPES pH 7.0, 0.15M ammonium sulfate
|
Resolution 2.29 Å R-free 0.247 |
| 5TVC Crystal structure of a chimeric acetylcholine binding protein from Aplysia californica (Ac-AChBP) containing loop C from the human alpha 3 nicotinic acetylcholine receptor in complex with (E,2S)-N-methyl-5-(5-phenoxy-3-pyridyl)pent-4-en-2-amine (TI-5312) Deposited 2016-11-08 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain A
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain B
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain C
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain D
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
18–198（181 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
Chain E
215–236（22 aa）
Fragment：UNP residues 18-198 + 215-236 from Aplysia californica linked by loop C (UNP residues 215-230) from Homo sapiens
|
Not recorded | SO4 SULFATE ION × 6 1PE PENTAETHYLENE GLYCOL × 1 7LB (E,2S)-N-methyl-5-(5-phenoxy-3-pyridyl)pent-4-en-2-amine × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；313 K；1.7% PEG 400, 0.085 M HEPES - Na pH 7.5, 1.7 M Ammonium Sulfate, 15% Glycerol
|
Resolution 1.93 Å R-free 0.225 |
| 5TVH Crystal structure of AChBP from Aplysia californica complex with 2-aminopyrimidine at pH 8.0 spacegroup P21 Deposited 2016-11-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–236（219 aa）
Chain B
18–236（219 aa）
Chain C
18–236（219 aa）
Chain D
18–236（219 aa）
Chain E
18–236（219 aa）
|
Not recorded | 7KO 6-chloro-N~4~,N~4~-bis[(pyridin-3-yl)methyl]pyrimidine-2,4-diamine × 5 DMS DIMETHYL SULFOXIDE × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；20% PEG 4000, 0.1M Tris pH 8.0, 0.2M NaCl
|
Resolution 2.40 Å R-free 0.247 |
| 5XGL Co-crystal structure of Ac-AChBPP in complex with alpha-conotoxin LvIA Deposited 2017-04-14 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
19–236（218 aa）
Chain B
19–236（218 aa）
Chain D
19–236（218 aa）
Chain G
19–236（218 aa）
Chain I
19–236（218 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M Bis-Tris propane PH 7.0
|
Resolution 3.44 Å R-free 0.283 |
| 6M4X Co-crystal structure of Ac-AChBPP in complex with [N9A]LvIA Deposited 2020-03-09 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
19–225（207 aa）
Chain B
19–225（207 aa）
Chain D
19–225（207 aa）
Chain G
19–225（207 aa）
Chain I
19–225（207 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；1.0 M Magnesium sulfate hydrate, 0.1 M Sodium acetate trihydrate (pH 4.6)
|
Resolution 3.00 Å R-free 0.316 |
| 6M4Z Co-crystal structure of Ac-AChBPP in complex with alpha-conotoxin [D11A]LvIA Deposited 2020-03-09 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric |
Chain A
19–225（207 aa）
Chain B
19–225（207 aa）
Chain D
19–225（207 aa）
Chain G
19–225（207 aa）
Chain I
19–225（207 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；1.2 M Sodium citrate tribasic dihydrate, 0.1 M BIS-TRIS propane (pH 7.0)
|
Resolution 2.80 Å R-free 0.268 |
| 6QKK Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (1) Deposited 2019-01-29 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | H92 4-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]benzamide × 5 PO4 PHOSPHATE ION × 5 EDO 1,2-ETHANEDIOL × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 OXL OXALATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl, 0.1 M Phosphate/citrate pH 4.2 12% PEG 8000
Buffer: 50 mM Tris, 250 mM NaCl pH 7.5
Protein concentration 4 mg/ml
Microseeded
|
Resolution 2.20 Å R-free 0.228 |
| 6QKK Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (1) Deposited 2019-01-29 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | H92 4-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]benzamide × 5 PO4 PHOSPHATE ION × 5 EDO 1,2-ETHANEDIOL × 20 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl, 0.1 M Phosphate/citrate pH 4.2 12% PEG 8000
Buffer: 50 mM Tris, 250 mM NaCl pH 7.5
Protein concentration 4 mg/ml
Microseeded
|
Resolution 2.20 Å R-free 0.228 |
| 6QQO Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (3) Deposited 2019-02-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | JC8 6-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]pyridine-3-carboxamide × 5 PO4 PHOSPHATE ION × 7 EDO 1,2-ETHANEDIOL × 24 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl 0.1 M Phosphate/citrate pH 4.2 10% PEG 8000
Buffer: 50 mM Tris 250 mM NaCl
Protein concentration 4 mg/ml
Microseeded
|
Resolution 2.50 Å R-free 0.212 |
| 6QQO Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (3) Deposited 2019-02-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | JC8 6-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]pyridine-3-carboxamide × 5 PO4 PHOSPHATE ION × 8 EDO 1,2-ETHANEDIOL × 18 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl 0.1 M Phosphate/citrate pH 4.2 10% PEG 8000
Buffer: 50 mM Tris 250 mM NaCl
Protein concentration 4 mg/ml
Microseeded
|
Resolution 2.50 Å R-free 0.212 |
| 6QQP Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (2) Deposited 2019-02-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | JCW 2-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]pyridine-4-carboxamide × 5 EDO 1,2-ETHANEDIOL × 31 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl, 0.1 M Phosphate/citrate pH 4.2 8% PEG 8000
Buffer: 50 mM Tris 250 mM NaCl pH 7.5
Protein concentration: 4 mg/ml
Microseeded
|
Resolution 2.40 Å R-free 0.210 |
| 6QQP Aplysia californica AChBP in complex with 2-Fluoro-(carbamoylpyridinyl)deschloroepibatidine analogue (2) Deposited 2019-02-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | JCW 2-[5-[(1~{R},2~{R},4~{S})-7-azabicyclo[2.2.1]heptan-2-yl]-2-fluoranyl-pyridin-3-yl]pyridine-4-carboxamide × 5 EDO 1,2-ETHANEDIOL × 29 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.2；293 K；Reservoir: 0.2 M NaCl, 0.1 M Phosphate/citrate pH 4.2 8% PEG 8000
Buffer: 50 mM Tris 250 mM NaCl pH 7.5
Protein concentration: 4 mg/ml
Microseeded
|
Resolution 2.40 Å R-free 0.210 |
| 6SGV Crystal structure of AcAChBP in complex with hosieine Deposited 2019-08-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 LDQ Hosieine × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；298 K；reservoir solution: 0.2 M CaCl2, 0.1M NaOAc pH 4.5, 16% isopropanol
Protein buffer: 50 mM tris pH 7.5, 250 mM NaCl, 4 mg/ml
mixed in 1ul protein : 2 ul reservoir
|
Resolution 2.60 Å R-free 0.257 |
| 6SGV Crystal structure of AcAChBP in complex with hosieine Deposited 2019-08-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | LDQ Hosieine × 5 ACT ACETATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.5；298 K；reservoir solution: 0.2 M CaCl2, 0.1M NaOAc pH 4.5, 16% isopropanol
Protein buffer: 50 mM tris pH 7.5, 250 mM NaCl, 4 mg/ml
mixed in 1ul protein : 2 ul reservoir
|
Resolution 2.60 Å R-free 0.257 |
| 6SH0 Crystal structure of AcAChBP in complex with anatoxin Deposited 2019-08-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
1–236（236 aa）
Chain B
1–236（236 aa）
Chain C
1–236（236 aa）
Chain D
1–236（236 aa）
Chain E
1–236（236 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 4 4P0 1-[(1R,6R)-9-azabicyclo[4.2.1]non-2-en-2-yl]ethanone × 5 ACT ACETATE ION × 3 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；Reservoir solution: 8% PEG 4K, 0.1 M NaOAc pH 4.6
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 4mg/ml
|
Resolution 2.50 Å R-free 0.289 |
| 6SH0 Crystal structure of AcAChBP in complex with anatoxin Deposited 2019-08-05 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain F
1–236（236 aa）
Chain G
1–236（236 aa）
Chain H
1–236（236 aa）
Chain I
1–236（236 aa）
Chain J
1–236（236 aa）
|
Not recorded | NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 GOL GLYCEROL × 1 4P0 1-[(1R,6R)-9-azabicyclo[4.2.1]non-2-en-2-yl]ethanone × 5 ACT ACETATE ION × 7 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；Reservoir solution: 8% PEG 4K, 0.1 M NaOAc pH 4.6
Protein buffer: 50 mM tris, 250 mM NaCl, pH 7.5, 4mg/ml
|
Resolution 2.50 Å R-free 0.289 |
| 6T9R Aplysia californica AChBP in complex with a cytisine derivative Deposited 2019-10-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain AAA
1–236（236 aa）
Chain BBB
1–236（236 aa）
Chain CCC
1–236（236 aa）
Chain DDD
1–236（236 aa）
Chain EEE
1–236（236 aa）
|
Not recorded | MXQ (1~{R},9~{S})-5-(3-oxidanylpropyl)-7,11-diazatricyclo[7.3.1.0^{2,7}]trideca-2,4-dien-6-one × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 21 PO4 PHOSPHATE ION × 5 CL CHLORIDE ION × 5 K POTASSIUM ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；295.15 K；Starting protein concentration 12.5 mg/ml + 6 mM ligand BS82.
Crystallised as hanging drops, the drop containing 1.5 ul protein, 0.2 ul reservoir (0.8 M NaH2PO4, 0.8 M KH2PO4, 10% glycerol, 0.1 M HEPES pH 7.0) and 0.3 ul microseeds from cytisine bound AChBP crystals (grown as sitting drops in 0.8 M NaH2PO4, 0.8 M KH2PO4, 0.1 M HEPES pH 7.5).
|
Resolution 1.72 Å R-free 0.192 |
| 6T9R Aplysia californica AChBP in complex with a cytisine derivative Deposited 2019-10-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain FFF
1–236（236 aa）
Chain GGG
1–236（236 aa）
Chain HHH
1–236（236 aa）
Chain III
1–236（236 aa）
Chain JJJ
1–236（236 aa）
|
Not recorded | MXQ (1~{R},9~{S})-5-(3-oxidanylpropyl)-7,11-diazatricyclo[7.3.1.0^{2,7}]trideca-2,4-dien-6-one × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 GOL GLYCEROL × 20 PO4 PHOSPHATE ION × 5 CL CHLORIDE ION × 5 K POTASSIUM ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7；295.15 K；Starting protein concentration 12.5 mg/ml + 6 mM ligand BS82.
Crystallised as hanging drops, the drop containing 1.5 ul protein, 0.2 ul reservoir (0.8 M NaH2PO4, 0.8 M KH2PO4, 10% glycerol, 0.1 M HEPES pH 7.0) and 0.3 ul microseeds from cytisine bound AChBP crystals (grown as sitting drops in 0.8 M NaH2PO4, 0.8 M KH2PO4, 0.1 M HEPES pH 7.5).
|
Resolution 1.72 Å R-free 0.192 |
| 7EGR Co-crystal structure of Ac-AChBPP in complex with RgIA Deposited 2021-03-26 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric |
Chain A
19–224（206 aa）
Chain B
20–223（204 aa）
Chain C
20–223（204 aa）
Chain D
19–224（206 aa）
Chain E
19–223（205 aa）
|
Not recorded | MG MAGNESIUM ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；1.8 M Magnesium sulfate hydrate, 0.1 M Sodium acetate trihydrate pH 4.6
|
Resolution 2.50 Å R-free 0.221 |
| 7EGR Co-crystal structure of Ac-AChBPP in complex with RgIA Deposited 2021-03-26 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric |
Chain F
19–223（205 aa）
Chain G
19–224（206 aa）
Chain H
19–224（206 aa）
Chain I
19–224（206 aa）
Chain J
19–224（206 aa）
|
Not recorded | MG MAGNESIUM ION × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；291 K；1.8 M Magnesium sulfate hydrate, 0.1 M Sodium acetate trihydrate pH 4.6
|
Resolution 2.50 Å R-free 0.221 |
| 8Q1M Aplysia californica acetylcholine-binding protein in complex with Spiroimine (+)-4 R Deposited 2023-07-31 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：UNP residues 18-225
Chain B
18–225（208 aa）
Fragment：UNP residues 18-225
Chain C
18–225（208 aa）
Fragment：UNP residues 18-225
Chain D
18–225（208 aa）
Fragment：UNP residues 18-225
Chain E
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | ILR Spiroimine (+)-4 R × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 CL CHLORIDE ION × 5 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；17% polyethylene glycol 4K (w/v), 0.1 M TRIS-HCL pH 7.5, 0.2 M sodium citrate pH 6.0, 10% glycerol 10% (v/v)
|
Resolution 2.00 Å R-free 0.206 |
| 8QTL Aplysia californica acetylcholine-binding protein in complex with Spiroimine (-)-4 S Deposited 2023-10-12 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：UNP residues 18-225
Chain B
18–225（208 aa）
Fragment：UNP residues 18-225
Chain C
18–225（208 aa）
Fragment：UNP residues 18-225
Chain D
18–225（208 aa）
Fragment：UNP residues 18-225
Chain E
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | WSP Spiroimine (-)-4 S × 5 CL CHLORIDE ION × 6 IPA ISOPROPYL ALCOHOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；15% polyethylene glycol 4K (w/v), 0.1 M HEPES pH 7.5, 10% isopropanol (v/v), 10% glycerol (v/v)
|
Resolution 1.85 Å R-free 0.211 |
| 8QX2 Aplysia californica acetylcholine-binding protein in complex with racemic spiroimine (+)/(-)-4 Deposited 2023-10-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric |
Chain A
18–225（208 aa）
Fragment：UNP residues 18-225
Chain B
18–225（208 aa）
Fragment：UNP residues 18-225
Chain C
18–225（208 aa）
Fragment：UNP residues 18-225
Chain D
18–225（208 aa）
Fragment：UNP residues 18-225
Chain E
18–225（208 aa）
Fragment：UNP residues 18-225
|
Not recorded | ILR Spiroimine (+)-4 R × 5 IPA ISOPROPYL ALCOHOL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.4；293 K；10% polyethylene glycol 1500 (w/v), 0.1 M sodium citrate buffer pH 5.5, 24% isopropanol (v/v)
|
Resolution 2.10 Å R-free 0.210 |
85 other PDB entries and 120 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | Q8WSF8_APLCA |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–212； UniProt 20–231 Author chain B； PDBConstruct 1–212； UniProt 20–231 Author chain C； PDBConstruct 1–212； UniProt 20–231 Author chain D； PDBConstruct 1–212； UniProt 20–231 Author chain E； PDBConstruct 1–212； UniProt 20–231 |
