Structure of PDB 1qh3 Chain B Binding Site BS04

Receptor Information
>1qh3 Chain B (length=260) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTV
LTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSL
NVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTAD
EMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA
KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRR
EKDQFKMPRD
Ligand information
Ligand IDACT
InChIInChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKeyQTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
SoftwareSMILES
ACDLabs 10.04[O-]C(=O)C
OpenEye OEToolkits 1.5.0CC(=O)[O-]
CACTVS 3.341CC([O-])=O
FormulaC2 H3 O2
NameACETATE ION
ChEMBL
DrugBankDB14511
ZINC
PDB chain1qh3 Chain B Residue 468 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1qh3 Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y175 R249 K252
Binding residue
(residue number reindexed from 1)		Y175 R249 K252
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H54 H56 D58 H59 H110 D134 H173
Catalytic site (residue number reindexed from 1) H54 H56 D58 H59 H110 D134 H173
Enzyme Commision number 3.1.2.6: hydroxyacylglutathione hydrolase.
Gene Ontology
Molecular Function
GO:0004416 hydroxyacylglutathione hydrolase activity
Biological Process
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione

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Molecular Function
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Biological Process
External links
PDB RCSB:1qh3, PDBe:1qh3, PDBj:1qh3
PDBsum1qh3
PubMed10508780
UniProtQ16775|GLO2_HUMAN Hydroxyacylglutathione hydrolase, mitochondrial (Gene Name=HAGH)

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