5HWL

Human glutathione s-transferase Mu2 complexed with BDEA, monoclinic crystal form

PDB DOI: https://doi.org/10.2210/pdb5HWL/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-01-29 Released: 2017-11-08
Deposition Author(s): Zhang, X., Wei, J., Wu, S., Zhang, H.P., Luo, M., Yang, X.L., Liao, F., Wang, D.Q.
Funding Organization(s): National Natural Science Foundation of China

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.60 Å
R-Value Free: 0.205
R-Value Work: 0.178
R-Value Observed: 0.179

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

Human glutathione s-transferase Mu2 complexed with BDEA, monoclinic crystal form

Zhang, X., Wei, J., Wu, S., Zhang, H.P., Luo, M., Yang, X.L., Liao, F., Wang, D.Q.

To be published.

Macromolecule Content

Total Structure Weight: 52.56 kDa
Atom Count: 3,798
Modelled Residue Count: 433
Deposited Residue Count: 434
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Glutathione S-transferase Mu 2	A, B	217	Homo sapiens	Mutation(s): 0 Gene Names: GSTM2, GST4 EC: 2.5.1.18
UniProt & NIH Common Fund Data Resources
Find proteins for P28161 (Homo sapiens) Explore P28161 Go to UniProtKB: P28161
PHAROS: P28161 GTEx: ENSG00000213366
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P28161
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
NNE Query on NNE Download Ideal Coordinates CCD File SDF format, chain E [auth B] MOL2 format, chain E [auth B]	E [auth B]	N,N'-(butane-1,4-diyl)bis{2-[2,3-dichloro-4-(2-methylidenebutanoyl)phenoxy]acetamide} C₃₀ H₃₂ Cl₄ N₂ O₆ DJUYDJABFNZJNL-UHFFFAOYSA-N		Interactions Focus chain E [auth B] Interactions & Density Focus chain E [auth B]
GSH Query on GSH 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]	GLUTATHIONE C₁₀ H₁₇ N₃ O₆ S RWSXRVCMGQZWBV-WDSKDSINSA-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: 1.60 Å
R-Value Free: 0.205
R-Value Work: 0.178
R-Value Observed: 0.179
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 50.97	α = 90
b = 48.89	β = 93.38
c = 90.99	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
PDB_EXTRACT	data extraction
MOSFLM	data reduction
SCALA	data scaling
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2017-11-08

Deposition Author(s):

Funding Organization	Location	Grant Number
National Natural Science Foundation of China	China	81301395

Revision History (Full details and data files)

Version 1.0: 2017-11-08
Type: Initial release
Version 1.1: 2023-11-08
Changes: Advisory, Data collection, Database references, Refinement description

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Help and Resources

5HWL

Human glutathione s-transferase Mu2 complexed with BDEA, monoclinic crystal form

Human glutathione s-transferase Mu2 complexed with BDEA, monoclinic crystal form

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)