Structure of PDB 1qh3 Chain A

Receptor sequence
>1qh3A (length=260) Species: 9606 (Homo sapiens) [Search protein sequence]
MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTV
LTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSL
NVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTAD
EMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA
KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRR
EKDQFKMPRD
3D structure
PDB1qh3 Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H54 H56 H110 D134 H54 H56 H110 D134
BS02 ZN A D58 H59 D134 H173 D58 H59 D134 H173
BS03 CAC A H56 H110 D134 Y145 H173 H56 H110 D134 Y145 H173
BS04 ACT A C141 Y175 R249 K252 C141 Y175 R249 K252
BS05 MN A H185 H235 E251 H185 H235 E251
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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