2OAC

Mouse C14A Glutathione-S-Transferase Mutant in Complex with S-(p-nitrobenzyl) Glutathione

PDB DOI: https://doi.org/10.2210/pdb2OAC/pdb

Classification: TRANSFERASE
Organism(s): Mus musculus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2006-12-15 Released: 2007-01-23
Deposition Author(s): Kyrieleis, O.J., McManus, G., Mantle, T.J., Khan, A.R.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.259
R-Value Work: 0.220
R-Value Observed: 0.228

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.6 of the entry. See complete history.

Literature

Structural and Kinetic Analyses of Glutathione S-Transferase Mutants

Kyrieleis, O.J., McManus, G., Mantle, T.J., Khan, A.R.

To be published.

Macromolecule Content

Total Structure Weight: 47.83 kDa
Atom Count: 3,547
Modelled Residue Count: 418
Deposited Residue Count: 418
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Glutathione S-transferase P 1	A, B	209	Mus musculus	Mutation(s): 1 Gene Names: Gstp1, Gstpib EC: 2.5.1.18
UniProt
Find proteins for P19157 (Mus musculus) Explore P19157 Go to UniProtKB: P19157
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P19157
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GTB Query on GTB Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	S-(P-NITROBENZYL)GLUTATHIONE C₁₇ H₂₂ N₄ O₈ S OAWORKDPTSAMBZ-STQMWFEESA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.259
R-Value Work: 0.220
R-Value Observed: 0.228
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 56.36	α = 90
b = 77.14	β = 90
c = 101.4	γ = 90

Software Package:

Software Name	Purpose
CNS	refinement
SCALEPACK	data scaling
REFMAC	refinement
PDB_EXTRACT	data extraction
CrystalClear	data collection
HKL-2000	data reduction
AMoRE	phasing
DENZO	data reduction

Structure Validation

View Full Validation Report

Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 2007-01-23

Deposition Author(s):

Kyrieleis, O.J.

Revision History (Full details and data files)

Version 1.0: 2007-01-23
Type: Initial release
Version 1.1: 2008-05-01
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-10-18
Changes: Refinement description
Version 1.4: 2019-07-24
Changes: Data collection, Refinement description
Version 1.5: 2021-10-20
Changes: Database references, Derived calculations
Version 1.6: 2023-08-30
Changes: Data collection, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.