5TF7

Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP

PDB DOI: https://doi.org/10.2210/pdb5TF7/pdb

Classification: HYDROLASE
Organism(s): Homo sapiens
Expression System: Escherichia coli 'BL21-Gold(DE3)pLysS AG
Mutation(s): Yes

Deposited: 2016-09-24 Released: 2018-05-09
Deposition Author(s): Wang, C., Aleksandrov, A.A., Yang, Z., Forouhar, F., Proctor, E., Kota, P., An, J., Kaplan, A., Khazanov, N., Boel, G., Stockwell, B.R., Senderowitz, H., Dokholyan, N.V., Riordan, J.R., Brouillette, C.G., Hunt, J.F.
Funding Organization(s): Cystic Fibrosis Foundation

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.93 Å
R-Value Free: 0.200
R-Value Work: 0.157
R-Value Observed: 0.161

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.1 of the entry. See complete history.

Literature

Thermodynamic correction of F508del-CFTR by ligand binding to a remote site in the mutated domain

Wang, C., Aleksandrov, A.A., Yang, Z., Forouhar, F., Proctor, E., Kota, P., An, J., Kaplan, A., Khazanov, N., Boel, G., Stockwell, B.R., Senderowitz, H., Dokholyan, N.V., Riordan, J.R., Brouillette, C.G., Hunt, J.F.

To be published.

Macromolecule Content

Total Structure Weight: 26.06 kDa
Atom Count: 1,870
Modelled Residue Count: 216
Deposited Residue Count: 229
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Cystic fibrosis transmembrane conductance regulator	A	229	Homo sapiens	Mutation(s): 1 Gene Names: CFTR, ABCC7 EC: 3.6.3.49 (PDB Primary Data), 5.6.1.6 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P13569 (Homo sapiens) Explore P13569 Go to UniProtKB: P13569
PHAROS: P13569 GTEx: ENSG00000001626
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P13569
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ATP Query on ATP Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	ADENOSINE-5'-TRIPHOSPHATE C₁₀ H₁₆ N₅ O₁₃ P₃ ZKHQWZAMYRWXGA-KQYNXXCUSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]
MG Query on MG Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.93 Å
R-Value Free: 0.200
R-Value Work: 0.157
R-Value Observed: 0.161
Space Group: P 4₃

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 40.288	α = 90
b = 40.288	β = 90
c = 141.165	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
HKL-2000	data processing
HKL-2000	data scaling

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2018-05-09

Deposition Author(s):

Funding Organization	Location	Grant Number
Cystic Fibrosis Foundation	United States	HUNT13XX0

Revision History (Full details and data files)

Version 1.0: 2018-05-09
Type: Initial release
Version 1.1: 2023-10-04
Changes: Author supporting evidence, Data collection, Database references, Refinement description

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Help and Resources

5TF7

Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP

Thermodynamic correction of F508del-CFTR by ligand binding to a remote site in the mutated domain

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)