2J9L

Cytoplasmic Domain of the Human Chloride Transporter ClC-5 in complex with ATP


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.263 
  • R-Value Observed: 0.264 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Nucleotide Recognition by the Cytoplasmic Domain of the Human Chloride Transporter Clc-5

Meyer, S.Savaresi, S.Forster, I.C.Dutzler, R.

(2006) Nat Struct Mol Biol 14: 60

  • DOI: https://doi.org/10.1038/nsmb1188
  • Primary Citation of Related Structures:  
    2J9L, 2JA3

  • PubMed Abstract: 

    The ubiquitous CBS domains, which are found as part of cytoplasmic domains in the ClC family of chloride channels and transporters, have previously been identified as building blocks for regulatory nucleotide-binding sites. Here we report the structures of the cytoplasmic domain of the human transporter ClC-5 in complex with ATP and ADP. The nucleotides bind to a specific site in the protein. As determined by equilibrium dialysis, the affinities for ATP, ADP and AMP are in the high micromolar range. Point mutations that interfere with nucleotide binding change the transport behavior of a ClC-5 mutant expressed in Xenopus laevis oocytes. Our results establish the structural and energetic basis for the interaction of ClC-5 with nucleotides and provide a framework for future investigations.


  • Organizational Affiliation

    Department of Biochemistry, University of Zurich, Winterthurer Strasse 190, CH-8057 Zurich, Switzerland.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CHLORIDE CHANNEL PROTEIN 5
A, B, C, D, E
A, B, C, D, E, F
185Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P51795 (Homo sapiens)
Explore P51795 
Go to UniProtKB:  P51795
PHAROS:  P51795
GTEx:  ENSG00000171365 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP51795
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
ATP
Query on ATP

Download Ideal Coordinates CCD File 
G [auth A]
I [auth B]
L [auth C]
N [auth D]
R [auth E]
G [auth A],
I [auth B],
L [auth C],
N [auth D],
R [auth E],
T [auth F]
ADENOSINE-5'-TRIPHOSPHATE
C10 H16 N5 O13 P3
ZKHQWZAMYRWXGA-KQYNXXCUSA-N
CL
Query on CL

Download Ideal Coordinates CCD File 
H [auth A]
J [auth B]
K [auth B]
M [auth C]
O [auth D]
H [auth A],
J [auth B],
K [auth B],
M [auth C],
O [auth D],
P [auth D],
Q [auth D],
S [auth E],
U [auth F],
V [auth F]
CHLORIDE ION
Cl
VEXZGXHMUGYJMC-UHFFFAOYSA-M
Binding Affinity Annotations 
IDSourceBinding Affinity
ATP Binding MOAD:  2J9L Kd: 9.00e+4 (nM) from 1 assay(s)
PDBBind:  2J9L Kd: 1.00e+5 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.30 Å
  • R-Value Free: 0.295 
  • R-Value Work: 0.263 
  • R-Value Observed: 0.264 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 122.328α = 90
b = 148.101β = 90
c = 79.883γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
TRUNCATEdata scaling
SHELXphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-01-04
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Refinement description, Version format compliance