2F5Y

Crystal Structure of the PDZ Domain from Human RGS-3

PDB DOI: https://doi.org/10.2210/pdb2F5Y/pdb

Deposited: 2005-11-28 Released: 2005-12-13
Deposition Author(s): Ugochukwu, E., Berridge, G., Johansson, C., Smee, C., Savitsky, P., Burgess, N., Colebrook, S., Yang, X., Elkins, J., Doyle, D., Turnbull, A., Papagrigoriou, E., Debreczeni, J., Bunkoczi, G., Gorrec, F., von Delft, F., Arrowsmith, C., Sundstrom, M., Weigelt, J., Edwards, A., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.39 Å
R-Value Free: 0.264
R-Value Work: 0.215
R-Value Observed: 0.217

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal Structure of the PDZ Domain from Human RGS-3

Ugochukwu, E., Berridge, G., Johansson, C., Smee, C., Savitsky, P., Burgess, N., Colebrook, S., Yang, X., Elkins, J., Doyle, D., Turnbull, A., Papagrigoriou, E., Debreczeni, J., Bunkoczi, G., Gorrec, F., von Delft, F., Arrowsmith, C., Sundstrom, M., Weigelt, J., Edwards, A.

To be published.

Macromolecule Content

Total Structure Weight: 20.67 kDa
Atom Count: 1,327
Modelled Residue Count: 164
Deposited Residue Count: 182
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
regulator of G-protein signalling 3 isoform 1	A, B	91	Homo sapiens	Mutation(s): 0 Gene Names: RGS3
UniProt & NIH Common Fund Data Resources
Find proteins for P49796 (Homo sapiens) Explore P49796 Go to UniProtKB: P49796
PHAROS: P49796 GTEx: ENSG00000138835
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P49796
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A]	C [auth A], D [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain C [auth A] Focus chain D [auth A] Interactions & Density Focus chain C [auth A] Focus chain D [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.39 Å
R-Value Free: 0.264
R-Value Work: 0.215
R-Value Observed: 0.217
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 91.11	α = 90
b = 44.14	β = 90
c = 49.857	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
PHASER	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2005-12-13

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2005-12-13
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.3: 2023-08-23
Changes: Data collection, Database references, Derived calculations, Refinement description

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Help and Resources

2F5Y

Crystal Structure of the PDZ Domain from Human RGS-3

Crystal Structure of the PDZ Domain from Human RGS-3

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)