Structure of PDB 2ab6 Chain A Binding Site BS01

Receptor Information

>2ab6 Chain A (length=217) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

PMTLGYWNIRGLAHSIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKF
KLGLDFPNLPYLIDGTHKITQSNAILRYIARKHNLCGESEKEQIREDILE
NQFMDSRMQLAKLCYDPDFEKLKPEYLQALPEMLKLYSQFLGKQPWFLGD
KITFVDFIAYDVLERNQVFEPSCLDAFPNLKDFISRFEGLEKISAYMKSS
RFLPRPVFTKMAVWGNK

Ligand information

Ligand ID

GSM

InChI

InChI=1S/C11H19N3O6S/c1-21-5-7(10(18)13-4-9(16)17)14-8(15)3-2-6(12)11(19)20/h6-7H,2-5,12H2,1H3,(H,13,18)(H,14,15)(H,16,17)(H,19,20)/t6-,7-/m0/s1

InChIKey

QTQDDTSVRVWHMO-BQBZGAKWSA-N

SMILES

Software	SMILES
CACTVS 3.341	CSC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O
CACTVS 3.341	CSC[CH](NC(=O)CC[CH](N)C(O)=O)C(=O)NCC(O)=O
OpenEye OEToolkits 1.5.0	CSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N
ACDLabs 10.04	O=C(NCC(=O)O)C(NC(=O)CCC(C(=O)O)N)CSC
OpenEye OEToolkits 1.5.0	CSCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N

Formula

C11 H19 N3 O6 S

Name

L-GAMMA-GLUTAMYL-S-METHYLCYSTEINYLGLYCINE;
S-METHYL-GLUTATHIONE

PDB chain

2ab6 Chain A Residue 1218 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2ab6 Expression, Crystallization and Preliminary X-Ray Analysis of Ligand-Free Human Glutathione S-Transferase M2-2
Resolution	2.5 Å
Binding residue (original residue number in PDB)	Y6 W7 L12 W45 K49 N58 L59 Q71 S72
Binding residue (residue number reindexed from 1)	Y6 W7 L12 W45 K49 N58 L59 Q71 S72
Annotation score	2

Enzymatic activity

Catalytic site (original residue number in PDB)	Y6 L12 R17
Catalytic site (residue number reindexed from 1)	Y6 L12 R17
Enzyme Commision number	2.5.1.18: glutathione transferase.

Gene Ontology

	Molecular Function
GO:0004364	glutathione transferase activity
GO:0004602	glutathione peroxidase activity
GO:0005102	signaling receptor binding
GO:0005504	fatty acid binding
GO:0005515	protein binding
GO:0016740	transferase activity
GO:0019899	enzyme binding
GO:0042802	identical protein binding
GO:0042803	protein homodimerization activity
GO:0043295	glutathione binding

	Biological Process
GO:0006629	lipid metabolic process
GO:0006749	glutathione metabolic process
GO:0010880	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
GO:0010881	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
GO:0014809	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
GO:0018916	nitrobenzene metabolic process
GO:0042178	xenobiotic catabolic process
GO:0043651	linoleic acid metabolic process
GO:0051122	hepoxilin biosynthetic process
GO:0055119	relaxation of cardiac muscle
GO:0060315	negative regulation of ryanodine-sensitive calcium-release channel activity
GO:0060316	positive regulation of ryanodine-sensitive calcium-release channel activity
GO:0070458	cellular detoxification of nitrogen compound
GO:0071313	cellular response to caffeine
GO:0098869	cellular oxidant detoxification

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0016529	sarcoplasmic reticulum
GO:0045171	intercellular bridge
GO:0070062	extracellular exosome

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Molecular Function

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Cellular Component

External links

PDB	RCSB:2ab6, PDBe:2ab6, PDBj:2ab6
PDBsum	2ab6
PubMed
UniProt	P28161\|GSTM2_HUMAN Glutathione S-transferase Mu 2 (Gene Name=GSTM2)

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