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8v7z

Phosphorylated, ATP-bound, E1371Q human cystic fibrosis transmembrane conductance regulator (E1371Q-CFTR)

Method: ELECTRON MICROSCOPY Dmax: 122.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Cystic fibrosis transmembrane conductance regulator

Homo sapiens

UniProt P13569

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 11–1431 Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.40 Å

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 8V7Z Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1XMI Crystal structure of human F508A NBD1 domain with ATP Deposited 2004-10-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 388–678（291 aa） Fragment：nucleotide binding domain one
Chain B 388–678（291 aa） Fragment：nucleotide binding domain one
Chain C 388–678（291 aa） Fragment：nucleotide binding domain one
Chain D 388–678（291 aa） Fragment：nucleotide binding domain one
Chain E 388–678（291 aa） Fragment：nucleotide binding domain one
Mutation：F508A Mutation：F508A Mutation：F508A Mutation：F508A Mutation：F508A MG MAGNESIUM ION × 5 ATP ADENOSINE-5'-TRIPHOSPHATE × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；PEG 400, glycerol, ethylene glycol, tris, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.25 Å R-free 0.265
1XMI Crystal structure of human F508A NBD1 domain with ATP Deposited 2004-10-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 388–678（291 aa） Fragment：nucleotide binding domain one
Chain B 388–678（291 aa） Fragment：nucleotide binding domain one
Chain C 388–678（291 aa） Fragment：nucleotide binding domain one
Chain D 388–678（291 aa） Fragment：nucleotide binding domain one
Chain E 388–678（291 aa） Fragment：nucleotide binding domain one
Mutation：F508A Mutation：F508A Mutation：F508A Mutation：F508A Mutation：F508A MG MAGNESIUM ION × 10 ATP ADENOSINE-5'-TRIPHOSPHATE × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；PEG 400, glycerol, ethylene glycol, tris, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.25 Å R-free 0.265
1XMJ Crystal structure of human deltaF508 human NBD1 domain with ATP Deposited 2004-10-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 388–678（291 aa） Fragment：nucleotide binding domain one
Mutation：deltaF508 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG 4000, glycerol, ethylene glycol, tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.30 Å R-free 0.287
2BBO Human NBD1 with Phe508 Deposited 2005-10-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 389–678（290 aa） Fragment：residues 389-678
Mutation：F409L, F429S, F433L, G550E, R553Q, R555K, H667R MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；280 K；30% PEG4000, 0.2M LiCl, 50mM Tris, pH 9, 3mM ATP, 5mM MgCl2, 2mM TCEP, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 280K
Resolution 2.55 Å R-free 0.274
2BBS Human deltaF508 NBD1 with three solubilizing mutations Deposited 2005-10-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 389–678（290 aa） Fragment：residues 389-678
Mutation：F429S, F494N, Q636R MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；280 K；39% PEG4000, 0.1M LiCl, 50mM Tris, pH 9.0, 3mM ATP, 5mM MgCl2, 2mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 280K
Resolution 2.05 Å R-free 0.291
2BBS Human deltaF508 NBD1 with three solubilizing mutations Deposited 2005-10-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 389–678（290 aa） Fragment：residues 389-678
Mutation：F429S, F494N, Q636R MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；280 K；39% PEG4000, 0.1M LiCl, 50mM Tris, pH 9.0, 3mM ATP, 5mM MgCl2, 2mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 280K
Resolution 2.05 Å R-free 0.291
2BBT Human deltaF508 NBD1 with two solublizing mutations. Deposited 2005-10-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 389–678（290 aa） Fragment：residues 389-678
Mutation：F504N, Q646R MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；280 K；35% PEG4000, 0.2M LiCl, 50mM Tris pH 7.5, 3mM ATP, 5mM MgCl2, 2mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 280K
Resolution 2.30 Å R-free 0.295
2BBT Human deltaF508 NBD1 with two solublizing mutations. Deposited 2005-10-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 389–678（290 aa） Fragment：residues 389-678
Mutation：F504N, Q646R MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；280 K；35% PEG4000, 0.2M LiCl, 50mM Tris pH 7.5, 3mM ATP, 5mM MgCl2, 2mM TCEP, VAPOR DIFFUSION, HANGING DROP, temperature 280K
Resolution 2.30 Å R-free 0.295
2LOB PDZ Domain of CAL (Cystic Fibrosis Transmembrane Regulator-Associated Ligand) Deposited 2012-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1473–1480（8 aa） Fragment：PDZ-binding motif residues 1473-1480
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；310 K；Ionic strength (raw mmCIF value) 1.0；Pressure ambient
NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] protein_1, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2PZE Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer Deposited 2007-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–404（18 aa） Fragment：CFTR NBD1 387-646(del405-436)
Chain A 437–646（210 aa） Fragment：CFTR NBD1 387-646(del405-436)
Mutation：del405-436 Mutation：del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 7.5, 25% PEG 6K; Cryo: 25% DMSO, vapor diffusion, temperature 281K
Resolution 1.70 Å R-free 0.247
2PZE Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer Deposited 2007-05-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 387–404（18 aa） Fragment：CFTR NBD1 387-646(del405-436)
Chain B 437–646（210 aa） Fragment：CFTR NBD1 387-646(del405-436)
Mutation：del405-436 Mutation：del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 7.5, 25% PEG 6K; Cryo: 25% DMSO, vapor diffusion, temperature 281K
Resolution 1.70 Å R-free 0.247
2PZF Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508 Deposited 2007-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–404（18 aa） Fragment：CFTR NBD1 387-646
Chain A 437–646（210 aa） Fragment：CFTR NBD1 387-646
Mutation：del405-436, delF508 Mutation：del405-436, delF508 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Tris pH 8.5, 35% PEG 4K, 0.2M NaAcetate; Cryo: 25% DMSO, vapor diffusion, temperature 281K
Resolution 2.00 Å R-free 0.251
2PZF Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508 Deposited 2007-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 387–404（18 aa） Fragment：CFTR NBD1 387-646
Chain B 437–646（210 aa） Fragment：CFTR NBD1 387-646
Mutation：del405-436, delF508 Mutation：del405-436, delF508 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Tris pH 8.5, 35% PEG 4K, 0.2M NaAcetate; Cryo: 25% DMSO, vapor diffusion, temperature 281K
Resolution 2.00 Å R-free 0.251
2PZF Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508 Deposited 2007-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 387–404（18 aa） Fragment：CFTR NBD1 387-646
Chain A 437–646（210 aa） Fragment：CFTR NBD1 387-646
Chain B 387–404（18 aa） Fragment：CFTR NBD1 387-646
Chain B 437–646（210 aa） Fragment：CFTR NBD1 387-646
Mutation：del405-436, delF508 Mutation：del405-436, delF508 Mutation：del405-436, delF508 Mutation：del405-436, delF508 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Tris pH 8.5, 35% PEG 4K, 0.2M NaAcetate; Cryo: 25% DMSO, vapor diffusion, temperature 281K
Resolution 2.00 Å R-free 0.251
2PZG Minimal human CFTR first nucleotide binding domain as a monomer Deposited 2007-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 375–404（30 aa） Fragment：CFTR NBD1 375-646(del405-436)
Chain A 437–646（210 aa） Fragment：CFTR NBD1 375-646(del405-436)
Mutation：del405-436 Mutation：del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 6.5, 25% PEG 10K ; Cryo: 25% glycerol, vapor diffusion, temperature 281K
Resolution 1.80 Å R-free 0.234
2PZG Minimal human CFTR first nucleotide binding domain as a monomer Deposited 2007-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 375–404（30 aa） Fragment：CFTR NBD1 375-646(del405-436)
Chain B 437–646（210 aa） Fragment：CFTR NBD1 375-646(del405-436)
Mutation：del405-436 Mutation：del405-436 MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；281 K；Protein: 9.5mg/ml NBD1, 0.15M NaCl, 0.01M methionine, 0.01M HEPES pH 7.5, 10% glycerol, 0.001M TCEP, 0.002M ATP; Well: 0.1M Hepes pH 6.5, 25% PEG 10K ; Cryo: 25% glycerol, vapor diffusion, temperature 281K
Resolution 1.80 Å R-free 0.234
3GD7 Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP) Deposited 2009-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain D 1193–1427（235 aa）
Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；1.1-1.25 M tri-sodium citrate, pH 5.5-8, sitting drop, temperature 277K, VAPOR DIFFUSION
Resolution 2.70 Å R-free 0.308
3GD7 Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP) Deposited 2009-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1193–1427（235 aa）
Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；1.1-1.25 M tri-sodium citrate, pH 5.5-8, sitting drop, temperature 277K, VAPOR DIFFUSION
Resolution 2.70 Å R-free 0.308
3GD7 Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP) Deposited 2009-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1193–1427（235 aa）
Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；1.1-1.25 M tri-sodium citrate, pH 5.5-8, sitting drop, temperature 277K, VAPOR DIFFUSION
Resolution 2.70 Å R-free 0.308
3GD7 Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP) Deposited 2009-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain C 1193–1427（235 aa）
Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；1.1-1.25 M tri-sodium citrate, pH 5.5-8, sitting drop, temperature 277K, VAPOR DIFFUSION
Resolution 2.70 Å R-free 0.308
3GD7 Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP) Deposited 2009-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 1193–1427（235 aa）
Chain B 1193–1427（235 aa）
Chain C 1193–1427（235 aa）
Chain D 1193–1427（235 aa）
Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D Mutation：Q1280E, Y1307N, E1308A, Q1309A, W1310H, H1402A, Q1411D B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；1.1-1.25 M tri-sodium citrate, pH 5.5-8, sitting drop, temperature 277K, VAPOR DIFFUSION
Resolution 2.70 Å R-free 0.308
3ISW Crystal structure of filamin-A immunoglobulin-like repeat 21 bound to an N-terminal peptide of CFTR Deposited 2009-08-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 5–22（18 aa） Fragment：UNP residues 5-22
Mutation：R21A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；0.1M Bis-Tris Propane pH 7.0, 60% Tacsimate, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.80 Å R-free 0.298
4WZ6 Human CFTR aa389-678 (NBD1), deltaF508 with three solubilizing mutations, bound ATP Deposited 2014-11-18 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 389–678（290 aa） Fragment：UNP residues 389-678
Mutation：F429S, F494N, deltaF508, Q637R ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；283 K；0.2M Magnesium Chloride, 0.1M Tris-HCl pH8.5, 33% PEG 4000
Resolution 2.05 Å R-free 0.239
5D2D Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768 Deposited 2015-08-05 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 747–774（28 aa） Fragment：UNP residues 747-774
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；277 K；HEPES, NaCl, DTT, Li2SO4, Glycine, K2HPO4
Resolution 2.10 Å R-free 0.220
5D3E Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795 Deposited 2015-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 762–801（40 aa） Fragment：UNP residues 762-801
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES, NaCl, DTT, (NH4)2SO4, Poly(acrylic acid sodium salt 2100
Resolution 2.75 Å R-free 0.244
5D3E Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795 Deposited 2015-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain G 762–801（40 aa） Fragment：UNP residues 762-801
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES, NaCl, DTT, (NH4)2SO4, Poly(acrylic acid sodium salt 2100
Resolution 2.75 Å R-free 0.244
5D3E Crystal structure of human 14-3-3 gamma in complex with CFTR R-domain peptide pS768-pS795 Deposited 2015-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain K 762–801（40 aa） Fragment：UNP residues 762-801
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；HEPES, NaCl, DTT, (NH4)2SO4, Poly(acrylic acid sodium salt 2100
Resolution 2.75 Å R-free 0.244
5D3F Crystal structure of human 14-3-3 zeta in complex with CFTR R-domain peptide pS753-pS768 and stabilizer fusicoccin-A Deposited 2015-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 747–774（28 aa） Fragment：UNP residues 747-774
Non-standard monomer：Yes (specific site not provided by mmCIF) FSC FUSICOCCIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；277 K；HEPES, NaCl, DTT, PEG6000
Resolution 2.74 Å R-free 0.303
5TF7 Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.93 Å R-free 0.200
5TF8 Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dTTP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M TTP THYMIDINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer:containing 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5, Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.86 Å R-free 0.187
5TFA Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dUTP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M DUT DEOXYURIDINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5; Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.87 Å R-free 0.195
5TFB Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with 7-methyl-GTP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 MGP 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5 Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.87 Å R-free 0.199
5TFC Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with GTP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5; Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.92 Å R-free 0.201
5TFD Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with CTP Deposited 2016-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 CTP CYTIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5; Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.89 Å R-free 0.195
5TFF Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with UTP Deposited 2016-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 UTP URIDINE 5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5; Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.89 Å R-free 0.190
5TFG Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with 5-methyl-UTP Deposited 2016-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 M5T 5-Methyluridine triphosphate × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；279 K；Protein buffer: 150 mM NaCl, 30% (v/v) glycerol, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5; Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.91 Å R-free 0.184
5TFI Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dGTP Deposited 2016-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 10% (v/v) glycerol,10% (v/v) Ethylene glycol, 10mM MgCl2, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5. Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.89 Å R-free 0.201
5TFJ Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dCTP Deposited 2016-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 DCP 2'-DEOXYCYTIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 10% (v/v) glycerol,10% (v/v) Ethylene glycol, 10mM MgCl2, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5. Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.85 Å R-free 0.185
5TGK Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with dATP Deposited 2016-09-28 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 387–646（260 aa） Fragment：Nucleotide-binding domain 1 (UNP residues 387-646)
Mutation：V470M MG MAGNESIUM ION × 1 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；pH 7.5；279 K；Protein buffer: 150 mM NaCl, 10% (v/v) glycerol,10% (v/v) Ethylene glycol, 10mM MgCl2, 1 mM TCEP, and 20 mM Na-HEPES, pH 7.5. Precipitant buffer: 40% (v/v) PEG 400, 100 mM NH4Cl, and 100 mM MES, pH 6
Resolution 1.91 Å R-free 0.198
5UAK Dephosphorylated, ATP-free human cystic fibrosis transmembrane conductance regulator (CFTR) Deposited 2016-12-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.87 Å
6HEP Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 Deposited 2018-08-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 747–774（28 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；278 K；0.1M Tris, 25% v/v PEG350 MME
Resolution 1.86 Å R-free 0.251
6HEP Crystal structure of human 14-3-3 beta in complex with CFTR R-domain peptide pS753-pS768 Deposited 2018-08-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 747–774（28 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；278 K；0.1M Tris, 25% v/v PEG350 MME
Resolution 1.86 Å R-free 0.251
6MSM Phosphorylated, ATP-bound human cystic fibrosis transmembrane conductance regulator (CFTR) Deposited 2018-10-16 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
6O1V Complex of human cystic fibrosis transmembrane conductance regulator (CFTR) and GLPG1837 Deposited 2019-02-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded LJP N-(3-carbamoyl-5,5,7,7-tetramethyl-4,7-dihydro-5H-thieno[2,3-c]pyran-2-yl)-1H-pyrazole-3-carboxamide × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
6O2P Complex of ivacaftor with cystic fibrosis transmembrane conductance regulator (CFTR) Deposited 2019-02-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 6 AJP Digitonin × 1 VX7 N-(2,4-di-tert-butyl-5-hydroxyphenyl)-4-oxo-1,4-dihydroquinoline-3-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
6RQR Extended NHERF1 PDZ2 domain in complex with the PDZ-binding motif of CFTR Deposited 2019-05-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1477–1480（4 aa）
Chain B 1477–1480（4 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；288 K；1.65 M ammonium sulphate, 100 mM tri-sodium citrate pH 5.6
Resolution 2.20 Å R-free 0.233
6UK1 Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Deposited 2019-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1202–1430（229 aa）
Mutation：S1255L,Q1280E,K1292D,Y1307N,K1334G,S1359A,Q1411D,H1402A,Q1411D ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；277 K；24% PEG 8000, 100 mM Li2SO4, 10mM NaBr, 100 mM Bis-Tris Propane pH 6.0
Resolution 2.69 Å R-free 0.304
6UK1 Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Deposited 2019-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1202–1430（229 aa）
Mutation：S1255L,Q1280E,K1292D,Y1307N,K1334G,S1359A,Q1411D,H1402A,Q1411D ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；277 K；24% PEG 8000, 100 mM Li2SO4, 10mM NaBr, 100 mM Bis-Tris Propane pH 6.0
Resolution 2.69 Å R-free 0.304
6UK1 Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Deposited 2019-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 1202–1430（229 aa）
Mutation：S1255L,Q1280E,K1292D,Y1307N,K1334G,S1359A,Q1411D,H1402A,Q1411D ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；277 K；24% PEG 8000, 100 mM Li2SO4, 10mM NaBr, 100 mM Bis-Tris Propane pH 6.0
Resolution 2.69 Å R-free 0.304
6UK1 Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Deposited 2019-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 1202–1430（229 aa）
Mutation：S1255L,Q1280E,K1292D,Y1307N,K1334G,S1359A,Q1411D,H1402A,Q1411D ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions MICROBATCH；277 K；24% PEG 8000, 100 mM Li2SO4, 10mM NaBr, 100 mM Bis-Tris Propane pH 6.0
Resolution 2.69 Å R-free 0.304
6WBS Human CFTR first nucleotide binding domain with dF508/V510D Deposited 2020-03-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 388–646（259 aa）
Mutation：deltaF508, V510D, delta405-436 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；CFTR NBD1 V510D in buffer A was crystallized by mixing equal amounts of protein at 6 mg/mL with 0.1 M Tris pH 7.6, 28% (w/v) polyethylene glycol 10,000. Crystallization was induced by streak-seeding using crystals grown in 0.1 M HEPES, pH 7.5, 25% (w/v) polyethylene glycol 550 monomethylether, and plates incubated at 4C. Crystals grew over several days and were frozen by quick dip in reservoir solution supplemented with 25% (w/v) ethylene glycol
Resolution 1.86 Å R-free 0.213
6WBS Human CFTR first nucleotide binding domain with dF508/V510D Deposited 2020-03-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 388–646（259 aa）
Mutation：deltaF508, V510D, delta405-436 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；CFTR NBD1 V510D in buffer A was crystallized by mixing equal amounts of protein at 6 mg/mL with 0.1 M Tris pH 7.6, 28% (w/v) polyethylene glycol 10,000. Crystallization was induced by streak-seeding using crystals grown in 0.1 M HEPES, pH 7.5, 25% (w/v) polyethylene glycol 550 monomethylether, and plates incubated at 4C. Crystals grew over several days and were frozen by quick dip in reservoir solution supplemented with 25% (w/v) ethylene glycol
Resolution 1.86 Å R-free 0.213
7QI1 Crystal structure of human 14-3-3 protein beta in complex with CFTR peptide pS753pS768 and PPI stabilizer CY007424 Deposited 2021-12-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: octameric
Chain E 747–774（28 aa）
Chain F 747–774（28 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) ARG ARGININE × 2 Q95 [2-(2-methylphenyl)sulfanylphenyl]methanamine × 2 TYR TYROSINE × 2 GLN GLUTAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；Qiagen Cryos Suite #44 (0.09 M HEPES sodium salt pH7.5, 1.26M tri-sodium citrate, 10% (v/v) glycerol) with an extra 2% (v/v) of glycerol.
Resolution 1.76 Å R-free 0.241
7SV7 The complex of phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP/Mg and Tezacaftor (VX-661) Deposited 2021-11-18 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 DD9 nonane × 2 D12 DODECANE × 4 CLR CHOLESTEROL × 2 C14 TETRADECANE × 1 PJ8 heptadecane × 1 CV6 Tezacaftor × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
7SVD The complex of phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP/Mg and Lumacaftor (VX-809) Deposited 2021-11-18 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 D12 DODECANE × 1 D10 DECANE × 2 CLR CHOLESTEROL × 3 VX8 Lumacaftor × 1 UNX UNKNOWN LIGAND × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
7SVR The complex of dephosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) and Lumacaftor (VX-809) Deposited 2021-11-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded VX8 Lumacaftor × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
8EIG The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with elexacaftor (VX-445) and ATP/Mg Deposited 2022-09-15 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CLR CHOLESTEROL × 1 WJX (6P)-N-(1,3-dimethyl-1H-pyrazole-4-sulfonyl)-6-[3-(3,3,3-trifluoro-2,2-dimethylpropoxy)-1H-pyrazol-1-yl]-2-[(4S)-2,2,4-trimethylpyrrolidin-1-yl]pyridine-3-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
8EIO The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with elexacaftor (VX-445), lumacaftor (VX-809) and ATP/Mg Deposited 2022-09-15 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CLR CHOLESTEROL × 1 D12 DODECANE × 1 VX8 Lumacaftor × 1 WJX (6P)-N-(1,3-dimethyl-1H-pyrazole-4-sulfonyl)-6-[3-(3,3,3-trifluoro-2,2-dimethylpropoxy)-1H-pyrazol-1-yl]-2-[(4S)-2,2,4-trimethylpyrrolidin-1-yl]pyridine-3-carboxamide × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
8EIQ The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with Trikafta [elexacaftor (VX-445), tezacaftor (VX-661), ivacaftor (VX-770)] and ATP/Mg Deposited 2022-09-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1370Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CLR CHOLESTEROL × 1 D12 DODECANE × 1 VX7 N-(2,4-di-tert-butyl-5-hydroxyphenyl)-4-oxo-1,4-dihydroquinoline-3-carboxamide × 1 WJX (6P)-N-(1,3-dimethyl-1H-pyrazole-4-sulfonyl)-6-[3-(3,3,3-trifluoro-2,2-dimethylpropoxy)-1H-pyrazol-1-yl]-2-[(4S)-2,2,4-trimethylpyrrolidin-1-yl]pyridine-3-carboxamide × 1 CV6 Tezacaftor × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8EJ1 Dephosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) Deposited 2022-09-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.90 Å
8FZQ Dehosphorylated, ATP-bound human cystic fibrosis transmembrane conductance regulator (CFTR) Deposited 2023-01-29 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 1–1480（1480 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.30 Å
8GLS Complex of human cystic fibrosis transmembrane conductance regulator (CFTR) and Z1834339853 Deposited 2023-03-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 ZRH (2S)-1-(3-amino-6-fluoro-1H-indazol-1-yl)-2-methyl-3-phenoxypropan-1-one × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
8UBR Complex of the phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with CFTRinh-172 and ATP/Mg Deposited 2023-09-24 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 LBN 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine × 2 CLR CHOLESTEROL × 2 WG5 4-[(Z)-{(3M)-4-oxo-2-sulfanylidene-3-[3-(trifluoromethyl)phenyl]-1,3-thiazolidin-5-ylidene}methyl]benzoic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
8V81 Phosphorylated, ATP-bound, inhibitor 172-bound E1371Q human cystic fibrosis transmembrane conductance regulator Deposited 2023-12-04 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 3–1440（1438 aa）
Mutation：E1371Q MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 5 CLR CHOLESTEROL × 1 WG5 4-[(Z)-{(3M)-4-oxo-2-sulfanylidene-3-[3-(trifluoromethyl)phenyl]-1,3-thiazolidin-5-ylidene}methyl]benzoic acid × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9DW4 Dephosphorylated CFTR in 1:1 complex with PKA-C (site II) Deposited 2024-10-08 Different construct Different mutation/modification 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 1–1480（1480 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.00 Å
9DW5 Dephosphorylated CFTR in 1:1 complex with PKA-C (site I) Deposited 2024-10-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Not recorded MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9DW7 Dephosphorylated CFTR in 1:2 complex with PKA-C Deposited 2024-10-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–1480（1480 aa）
Not recorded MG MAGNESIUM ION × 2 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.00 Å
9DW8 Dephosphorylated (E1371Q)CFTR in complex with PKA-C Deposited 2024-10-08 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q B44 N-(2-phenylethyl)adenosine 5'-(tetrahydrogen triphosphate) × 2 MG MAGNESIUM ION × 4 ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9DW9 Phosphorylated (E1371Q)CFTR in complex with PKA-C Deposited 2024-10-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–1480（1480 aa）
Mutation：E1371Q Non-standard monomer：Yes (specific site not provided by mmCIF) CLR CHOLESTEROL × 1 D10 DECANE × 4 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 3 CL CHLORIDE ION × 4 UND UNDECANE × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
9MXL Complex of the phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with (R)-BPO-27 and ATP/Mg Deposited 2025-01-20 Different construct Different ligand/ion Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–1480（1480 aa）
Mutation：E1371Q A1BUJ (6R,12R)-6-(5-bromofuran-2-yl)-7,9-dimethyl-8,10-dioxo-11-phenyl-7,8,9,10-tetrahydro-6H-pyrimido[4',5':3,4]pyrrolo[2,1-c][1,4]benzoxazine-2-carboxylic acid × 1 MG MAGNESIUM ION × 2 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 CL CHLORIDE ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.10 Å

52 other PDB entries and 70 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CFTR_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–1421； UniProt 11–1431

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8v7z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v7z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v7z
Deposition date deposition_date2023-12-04
Structure title titlePhosphorylated, ATP-bound, E1371Q human cystic fibrosis transmembrane conductance regulator (E1371Q-CFTR)
Keywords keywordscystic fibrosis, chloride channel, hydrolysis-deficient mutant, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.09 Å
Radius of gyration Rg (electron density) rg_electron35.47 Å
Forward intensity I(0) i0212074000.00
Molecular weight molecular_weight127490.0 kDa
Excluded volume excluded_volume163860 ų
Envelope volume envelope_volume201850 ų
Hydration-shell volume shell_volume48162 ų
Envelope diameter envelope_diameter129.7 Å
Shell Rg shell_rg41.16 Å
Envelope Rg envelope_rg35.71 Å
Shape Rg shape_rg35.46 Å
Total Rg total_rg35.89 Å
Total atoms total_atoms8977
Residues n_residues1104
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax122.0 Å
Rg (real space) rg_real35.29 Å
Rg uncertainty (real space) rg_real_error1.05 Å
I(0) (real space) i0_real2.1210e+08
I(0) uncertainty (real space) i0_real_error3.7030e+06
Rg (reciprocal space) rg_reciprocal35.17 Å
I(0) (reciprocal space) i0_reciprocal212100000.0000
Solution quality estimate total_estimate0.8454
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.2 Å
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis-0.149
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60970000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.723; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.882
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)