Structure of PDB 1qh3 Chain A Binding Site BS05
Receptor Information
>1qh3 Chain A (length=260) Species:
9606
(Homo sapiens) [
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MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAARKHGVKLTTV
LTTHHHWDHAGGNEKLVKLESGLKVYGGDDRIGALTHKITHLSTLQVGSL
NVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTAD
EMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA
KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETDPVTTMRAVRR
EKDQFKMPRD
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
1qh3 Chain A Residue 266 [
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Receptor-Ligand Complex Structure
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PDB
1qh3
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
H185 H235 E251
Binding residue
(residue number reindexed from 1)
H185 H235 E251
Annotation score
1
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
PDBsum
1qh3
PubMed
10508780
UniProt
Q16775
|GLO2_HUMAN Hydroxyacylglutathione hydrolase, mitochondrial (Gene Name=HAGH)
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