Complement factor D
Homo sapiens
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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count | Chain A； UniProt 26–253 | Fragment：UNP residues 26-253 | GOL GLYCEROL × 1 5W5 methyl 2-[[[(2~{S})-2-[[3-(trifluoromethyloxy)phenyl]carbamoyl]pyrrolidin-1-yl]carbonylamino]methyl]benzoate × 1 | X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；293 K；1 MICROLITER PROTEIN SOLUTION WAS MIXED WITH 1 MICROLITER RESERVOIR SOLUTION. PROTEIN SOLUTION: 18 mg/mL FD, 10 mM Tris pH 7.0, 100 mM NaCl; RESERVOIR SOLUTION: 22% PEG3350, 100 mM HEPES pH 7.5; SOAKING AND CRYO: ADDITION of 10 mM COMPOUND2 for 45 min FOLLOWED by the ADDITION OF 0.5 MICROLITER GLYCEROL AND FLASH FREEZING IN LIQUIT NITROGEN. | Resolution 1.43 Å R-free 0.188 |
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 5FBE | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1BIO HUMAN COMPLEMENT FACTOR D IN COMPLEX WITH ISATOIC ANHYDRIDE INHIBITOR Deposited 1998-06-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | SOA ISATOIC ANHYDRIDE × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.4；pH 6.4
|
Resolution 1.50 Å R-free 0.191 |
| 1DFP FACTOR D INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE Deposited 1997-02-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
26–253（228 aa）
Chain B
26–253（228 aa）
|
Not recorded | DFP DIISOPROPYL PHOSPHONATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.8；INHIBITED PROTEIN WAS CRYSTALLIZED FROM 12-16% PEG 6000 AND 0.2 M NACL,50MM MES BUFFER, PH=5.6-5.8.
|
Resolution 2.40 Å R-free 0.228 |
| 1DIC STRUCTURE OF 3,4-DICHLOROISOCOUMARIN-INHIBITED FACTOR D Deposited 1998-07-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | DIC 3,4-DICHLOROISOCOUMARIN × 1 O OXYGEN ATOM × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.6；pH 5.6
|
Resolution 1.80 Å R-free 0.251 |
| 1DST MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY Deposited 1995-09-13 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Mutation：S94Y, T214S, S215W | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6.8；pH 6.8
|
Resolution 2.00 Å R-free 0.213 |
| 1DSU HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME Deposited 1995-09-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
26–253（228 aa）
Chain B
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.00 Å R-free 0.203 |
| 1FDP PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D Deposited 1998-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
19–253（235 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000
AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION
AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.251 |
| 1FDP PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D Deposited 1998-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
19–253（235 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000
AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION
AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.251 |
| 1FDP PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D Deposited 1998-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
19–253（235 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000
AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION
AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.251 |
| 1FDP PROENZYME OF HUMAN COMPLEMENT FACTOR D, RECOMBINANT PROFACTOR D Deposited 1998-12-03 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
19–253（235 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.2；298 K；CRYSTALLIZATION CONDITIONS: THE RESERVOIR SOLUTION CONTAINED 10-12% PEG-6000
AND 30MM MES (PH5.2). THE DROPS CONTAINED EQUAL VOLUME OF RESERVOIR SOLUTION
AND PROTEIN SOLUTION (10MG/ML), VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 2.10 Å R-free 0.251 |
| 1HFD HUMAN COMPLEMENT FACTOR D IN A P21 CRYSTAL FORM Deposited 1998-06-18 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 5.4；pH 5.4
|
Resolution 2.30 Å R-free 0.216 |
| 2XW9 Crystal Structure of Complement Factor D mutant S183A Deposited 2010-11-01 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Mutation：YES | GOL GLYCEROL × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；pH 6.0
|
Resolution 1.20 Å R-free 0.176 |
| 2XWA Crystal Structure of Complement Factor D Mutant R202A Deposited 2010-11-01 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Mutation：YES | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；pH 6.0
|
Resolution 2.80 Å R-free 0.283 |
| 2XWA Crystal Structure of Complement Factor D Mutant R202A Deposited 2010-11-01 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
|
Mutation：YES | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；pH 6.0
|
Resolution 2.80 Å R-free 0.283 |
| 2XWB Crystal Structure of Complement C3b in complex with Factors B and D Deposited 2010-11-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain J
26–253（228 aa）
|
Mutation：YES | MG MAGNESIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.7；PH 7.7
|
Resolution 3.49 Å R-free 0.244 |
| 2XWB Crystal Structure of Complement C3b in complex with Factors B and D Deposited 2010-11-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain I
26–253（228 aa）
|
Mutation：YES | MG MAGNESIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.7；PH 7.7
|
Resolution 3.49 Å R-free 0.244 |
| 2XWB Crystal Structure of Complement C3b in complex with Factors B and D Deposited 2010-11-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain J
26–253（228 aa）
|
Mutation：YES | MG MAGNESIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.7；PH 7.7
|
Resolution 3.49 Å R-free 0.244 |
| 2XWB Crystal Structure of Complement C3b in complex with Factors B and D Deposited 2010-11-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain I
26–253（228 aa）
|
Mutation：YES | MG MAGNESIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 7.7；PH 7.7
|
Resolution 3.49 Å R-free 0.244 |
| 4CBN Crystal structure of Complement Factor D mutant R202A after conventional refinement Deposited 2013-10-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
Fragment：RESIDUES 26-253
|
Mutation：YES | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
15% PEG 6000, 50 MM MES/NAOH, PH 6.0
|
Resolution 1.80 Å R-free 0.219 |
| 4CBN Crystal structure of Complement Factor D mutant R202A after conventional refinement Deposited 2013-10-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
Fragment：RESIDUES 26-253
|
Mutation：YES | GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
15% PEG 6000, 50 MM MES/NAOH, PH 6.0
|
Resolution 1.80 Å R-free 0.219 |
| 4CBO Crystal structure of Complement Factor D mutant R202A after ensemble refinement Deposited 2013-10-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
Fragment：RESIDUES 26-253
|
Mutation：YES | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
15% PEG 6000, 50 MM MES/NAOH PH 6.0
|
Resolution 1.80 Å R-free 0.212 |
| 4CBO Crystal structure of Complement Factor D mutant R202A after ensemble refinement Deposited 2013-10-15 | Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
Fragment：RESIDUES 26-253
|
Mutation：YES | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
15% PEG 6000, 50 MM MES/NAOH PH 6.0
|
Resolution 1.80 Å R-free 0.212 |
| 4D9R Inhibiting Alternative Pathway Complement Activation by Targeting the Exosite on Factor D Deposited 2012-01-11 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris-HCl, 0.02 M NH4PO4, MPD 50.0% v/v, 0.01 M hexamine cobalt (III) chloride, pH 8.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 2.42 Å R-free 0.251 |
| 4D9R Inhibiting Alternative Pathway Complement Activation by Targeting the Exosite on Factor D Deposited 2012-01-11 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain B
26–253（228 aa）
|
Not recorded | CL CHLORIDE ION × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1 M Tris-HCl, 0.02 M NH4PO4, MPD 50.0% v/v, 0.01 M hexamine cobalt (III) chloride, pH 8.5, vapor diffusion, hanging drop, temperature 277K
|
Resolution 2.42 Å R-free 0.251 |
| 5FBI COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 3b Deposited 2015-12-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 5WD 3-[(2-aminocarbonyl-1~{H}-indol-5-yl)oxymethyl]benzoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；1 Microliter of protein solution was mixed with 1 microliter of reservoir solution. Protein solution: 18.3 mg/ml factor D, 10 mM Tris pH 7.0, 100 mM sodium chloride; Reservoir solution: 22% PEG3350, 100 mM HEPES pH 7.5; Soaking and cryo: 0.5 ul 100 mM compound 3b in 90% DMSO was added to the crystal containing drop and incubated for 45 min followed by the addition of 0.5 ul glyerol and flash freezing in liquid nitrogen.
|
Resolution 1.47 Å R-free 0.196 |
| 5FCK COMPLEMENT FACTOR D IN COMPLEX WITH COMPOUND 5 Deposited 2015-12-15 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | 5WC 1-[2-[(1~{R},3~{S},5~{R})-3-[[(1~{R})-1-(3-chloranyl-2-fluoranyl-phenyl)ethyl]carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxidanylidene-ethyl]pyrazolo[3,4-c]pyridine-3-carboxamide × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293 K；1 uL FD solution (18 mg/mL FD, 10 mM Tris pH 7.0, 100 mM NaCl) was mixed with 1 uL reservoir solution (25% PEG3350, 100 mM TRIS pH 8.0) and equilibrated against 1 mL reservoir solution.
|
Resolution 1.86 Å R-free 0.237 |
| 5MT0 COMPLEMENT FACTOR D IN COMPLEX WITH A REVERSIBLE INDOLE CARBOXYLIC ACID BASED INHIBITOR Deposited 2017-01-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | QJS 5-fluoranyl-3-[[(1~{S},2~{S})-2-phenylcyclopropyl]carbonylamino]-1~{H}-indole-2-carboxylic acid × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM BIS-TRIS pH 6.5
|
Resolution 1.29 Å R-free 0.196 |
| 5MT4 COMPLEMENT FACTOR D IN COMPLEX WITH A REVERSIBLE BENZOIC ACID BASED INHIBITOR Deposited 2017-01-06 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | M7O 2-[(phenylmethyl)carbamoylamino]benzoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；26% PEGME2000, 100mM Bis-Tris pH 6.5
|
Resolution 1.65 Å R-free 0.239 |
| 5NAR Complement factor D in complex with the inhibitor (S)-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide] Deposited 2017-02-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | SO4 SULFATE ION × 1 8RW (2~{S})-~{N}1-(1-aminocarbonylindol-3-yl)-~{N}2-[3-(trifluoromethyloxy)phenyl]pyrrolidine-1,2-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；MM NACL, 0.5MM NVP-BVT244-NX-1
+ 1 UL RESERVOIR SOLUTION
|
Resolution 1.55 Å R-free 0.231 |
| 5NAT Complement factor D in complex with the inhibitor (S)-Pyrrolidine-1,2-dicarboxylic acid 1-[(1-methyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide] Deposited 2017-02-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 2 8RT (2~{S})-~{N}1-(1-methylindol-3-yl)-~{N}2-[3-(trifluoromethyloxy)phenyl]pyrrolidine-1,2-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；MM NACL
+ 1 UL RESERVOIR SOLUTION
|
Resolution 1.17 Å |
| 5NAW Complement factor D in complex with the inhibitor (1R,3S,5R)-2-Aza-bicyclo[3.1.0]hexane-2,3-dicarboxylic acid 2-[(1-carbamoyl-1H-indol-3-yl)-amide] 3-[(3-trifluoromethoxy-phenyl)-amide] Deposited 2017-02-28 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | 8RZ (1~{R},3~{S},5~{R})-~{N}2-(1-aminocarbonylindol-3-yl)-~{N}3-[3-(trifluoromethyloxy)phenyl]-2-azabicyclo[3.1.0]hexane-2,3-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；27% PEG 3350
100 mM HEPES pH 7.5
|
Resolution 1.25 Å R-free 0.178 |
| 5NB6 Complement factor D in complex with the inhibitor (2S,4S)-4-Amino-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide] Deposited 2017-03-01 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | 8S2 (2~{S},4~{S})-~{N}1-(1-aminocarbonylindol-3-yl)-4-azanyl-~{N}2-[3-(trifluoromethyloxy)phenyl]pyrrolidine-1,2-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；22% PEG3350, 0.1 M HEPES pH 7.5, 50 mM NaCl
|
Resolution 1.75 Å R-free 0.297 |
| 5NB7 Complement factor D Deposited 2017-03-01 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | DMS DIMETHYL SULFOXIDE × 2 8NQ 1-[2-[(1~{R},3~{S},5~{R})-3-[(6-bromanylpyridin-2-yl)carbamoyl]-2-azabicyclo[3.1.0]hexan-2-yl]-2-oxidanylidene-ethyl]indazole-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；298 K；22% PEG 3350, 0.1 m HEPES pH 7.5, 50 mM NaCl
|
Resolution 1.33 Å R-free 0.196 |
| 5NBA Complement factor D in complex with the inhibitor (2S,4R)-4-Fluoro-pyrrolidine-1,2-dicarboxylic acid 1-[(1-carbamoyl-1H-indol-3-yl)-amide] 2-[(3-trifluoromethoxy-phenyl)-amide] Deposited 2017-03-01 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | 8S5 (2~{S},4~{R})-~{N}1-(1-aminocarbonylindol-3-yl)-4-fluoranyl-~{N}2-[3-(trifluoromethyloxy)phenyl]pyrrolidine-1,2-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；23% PEG 3350, 0.1 M HEPES pH 7.5, 50 mM NaCl
|
Resolution 1.87 Å R-free 0.260 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain F
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCA Complement Factor D inhibited with JH3 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain G
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J55 1-(2-{(2S)-2-[(6-bromopyridin-2-yl)carbamoyl]-1,3-thiazolidin-3-yl}-2-oxoethyl)-1H-pyrazolo[3,4-b]pyridine-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1 M Tris-HCl pH 8.5, 15% PEG 20000
|
Resolution 3.15 Å R-free 0.264 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain F
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 5TCC Complement Factor D inhibited with JH4 Deposited 2016-09-14 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 7 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain G
26–253（228 aa）
Fragment：residues 26-253
|
Not recorded | J56 (2S)-N-(6-bromopyridin-2-yl)-3-[(1H-indazol-1-yl)acetyl]-1,3-thiazolidine-2-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；0.1 M MES pH 6.5 and 25% PEG 8000
|
Resolution 3.37 Å R-free 0.260 |
| 6FTY COMPLEMENT FACTOR D COMPLEXED WITH COMPOUND 5 Deposited 2018-02-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E7H 4-[[(5~{S},7~{R})-3-azanyl-1-adamantyl]carbonylamino]-1~{H}-indole-2-carboxamide × 1 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；295 K；PEG 3350, 100 mM HEPES pH 7.5
|
Resolution 1.67 Å R-free 0.214 |
| 6FTZ COMPLEMENT FACTOR D COMPLEXED WITH COMPOUND 6 Deposited 2018-02-26 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E7E ~{N}4-[3-(aminomethyl)phenyl]-1~{H}-indole-2,4-dicarboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；295 K；PEG3350, 100 mM HEPES pH 7.5
|
Resolution 1.67 Å R-free 0.220 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUG Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain F
26–253（228 aa）
|
Not recorded | E85 3-[[3-[[3-(aminomethyl)phenyl]amino]-1~{H}-pyrazolo[3,4-d]pyrimidin-4-yl]amino]phenol × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5
|
Resolution 2.21 Å R-free 0.259 |
| 6FUH Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinazolin-2-yl)-L-valine Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E88 (2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]-3-methyl-butanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；25% PEG3350, 100 mM TRIS pH 8.5, 200 mM NH4SO2, 2 mM inhibitor
|
Resolution 1.37 Å R-free 0.180 |
| 6FUI Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino)phenol Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E7W (1~{R},2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]cyclohexane-1-carboxylic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5
|
Resolution 1.38 Å R-free 0.198 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E8B ~{N}-[3-[3-(aminomethyl)phenyl]phenyl]-3-methyl-butanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
|
Not recorded | E8B ~{N}-[3-[3-(aminomethyl)phenyl]phenyl]-3-methyl-butanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
26–253（228 aa）
|
Not recorded | E8B ~{N}-[3-[3-(aminomethyl)phenyl]phenyl]-3-methyl-butanamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUJ Complement factor D in complex with the inhibitor N-(3'-(aminomethyl)-[1,1'-biphenyl]-3-yl)-3-methylbutanamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain F
26–253（228 aa）
|
Not recorded | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5, 2 mM inhibitor
|
Resolution 2.25 Å R-free 0.244 |
| 6FUT Complement factor D in complex with the inhibitor (S)-3'-(aminomethyl)-N-(1,2,3,4-tetrahydronaphthalen-1-yl)-[1,1'-biphenyl]-3-carboxamide Deposited 2018-02-27 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | E82 3-[3-(aminomethyl)phenyl]-~{N}-[(1~{S})-1,2,3,4-tetrahydronaphthalen-1-yl]benzamide × 1 SIN SUCCINIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；22-25% PEG3350, 100 mM HEPES pH 7.5
|
Resolution 1.50 Å R-free 0.184 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain E
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMR Complement factor D in complex with the inhibitor (S)-2-(2-((3'-(1-amino-2-hydroxyethyl)-[1,1'-biphenyl]-3-yl)methoxy)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain F
2–253（252 aa）
|
Not recorded | J6T 2-[2-[[3-[3-[(1~{S})-1-azanyl-2-oxidanyl-ethyl]phenyl]phenyl]methoxy]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；293 K；30% PEG MME 2000, 0.1M sodium thiocyanate
|
Resolution 2.00 Å R-free 0.256 |
| 6QMT Complement factor D in complex with the inhibitor 2-(2-(3'-(aminomethyl)-[1,1'-biphenyl]-3-carboxamido)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
2–253（252 aa）
|
Not recorded | J7B 2-[2-[[3-[3-(aminomethyl)phenyl]phenyl]carbonylamino]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；25% PEGME 3350, 100 mM Bis-Tris pH 5.5
|
Resolution 1.80 Å R-free 0.231 |
| 6QMT Complement factor D in complex with the inhibitor 2-(2-(3'-(aminomethyl)-[1,1'-biphenyl]-3-carboxamido)phenyl)acetic acid Deposited 2019-02-08 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
2–253（252 aa）
|
Not recorded | J7B 2-[2-[[3-[3-(aminomethyl)phenyl]phenyl]carbonylamino]phenyl]ethanoic acid × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；25% PEGME 3350, 100 mM Bis-Tris pH 5.5
|
Resolution 1.80 Å R-free 0.231 |
| 6VMJ Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain Z
26–253（228 aa）
|
Not recorded | CIT CITRIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M sodium cacodylate pH 6.5, 1 M sodium citrate
|
Resolution 2.95 Å R-free 0.265 |
| 6VMJ Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain Y
26–253（228 aa）
|
Not recorded | CIT CITRIC ACID × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M sodium cacodylate pH 6.5, 1 M sodium citrate
|
Resolution 2.95 Å R-free 0.265 |
| 6VMJ Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain X
26–253（228 aa）
|
Not recorded | CIT CITRIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M sodium cacodylate pH 6.5, 1 M sodium citrate
|
Resolution 2.95 Å R-free 0.265 |
| 6VMJ Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain W
26–253（228 aa）
|
Not recorded | CIT CITRIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；0.1 M sodium cacodylate pH 6.5, 1 M sodium citrate
|
Resolution 2.95 Å R-free 0.265 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain W
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 10 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain d
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 11 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain g
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 12 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain j
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 13 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain m
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 14 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain p
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 15 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain s
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 16 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain v
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain C
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain F
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain I
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain N
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain Q
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain T
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain X
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 SO4 SULFATE ION × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 6VMK Crystal structure of human Complement Factor D with anti-Factor D Fab 20D12 Deposited 2020-01-28 | Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 9 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain a
26–253（228 aa）
|
Not recorded | GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；0.1 M sodium citrate pH 5.0, 8% PEG 8000
|
Resolution 3.01 Å R-free 0.215 |
| 8D95 Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-09 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | QIE N-(6-bromopyridin-2-yl)-1-[(3-cyanophenyl)acetyl]-L-prolinamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；300 K；PEG 6k
|
Resolution 2.17 Å R-free 0.263 |
| 8DEA Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | R7X 1-[(3-acetylphenyl)acetyl]-N-(6-bromopyridin-2-yl)-L-prolinamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；peg4k 25% , 0.1M MES 5.8 buffer
|
Resolution 2.21 Å R-free 0.300 |
| 8DEA Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain B
26–253（228 aa）
|
Not recorded | R7X 1-[(3-acetylphenyl)acetyl]-N-(6-bromopyridin-2-yl)-L-prolinamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；peg4k 25% , 0.1M MES 5.8 buffer
|
Resolution 2.21 Å R-free 0.300 |
| 8DEA Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain C
26–253（228 aa）
|
Not recorded | R7X 1-[(3-acetylphenyl)acetyl]-N-(6-bromopyridin-2-yl)-L-prolinamide × 1 GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；peg4k 25% , 0.1M MES 5.8 buffer
|
Resolution 2.21 Å R-free 0.300 |
| 8DEA Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-20 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain D
26–253（228 aa）
|
Not recorded | R7X 1-[(3-acetylphenyl)acetyl]-N-(6-bromopyridin-2-yl)-L-prolinamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；293 K；peg4k 25% , 0.1M MES 5.8 buffer
|
Resolution 2.21 Å R-free 0.300 |
| 8DG6 Scaffold Hopping via Ring Opening Enables Identification of Acyclic Compounds as New Complement Factor D Inhibitors Deposited 2022-06-23 | Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
26–253（228 aa）
|
Not recorded | S7X 1-{2-[(2S)-2-{[(3-chloro-2-fluorophenyl)methyl]carbamoyl}pyrrolidin-1-yl]-2-oxoethyl}-1H-indazole-3-carboxamide × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 5.8；300 K；peg4k 20-30%
|
Resolution 1.99 Å R-free 0.251 |
39 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | CFAD_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–228； UniProt 26–253 |
