Structure of PDB 4x2a Chain B

Receptor sequence
>4x2aB (length=175) Species: 10090 (Mus musculus) [Search protein sequence]
SSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTL
LQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGT
EDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGM
KGLAFIQDPDGYWIEILNPNKIATI
3D structure
PDB4x2a In Vitro Inhibition of Glyoxalase І by Flavonoids: New Insights from Crystallographic Analysis.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q34 E100 H127 E173
Catalytic site (residue number reindexed from 1) Q27 E93 H120 E165
Enzyme Commision number 4.4.1.5: lactoylglutathione lyase.
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 B Q34 E100 Q27 E93
BS02 ZN B H127 E173 H120 E165
BS03 3WL B Q34 F63 F68 L70 F93 E100 Q27 F56 F61 L63 F86 E93 MOAD: Ki=0.183uM
BS04 3WL B H127 M158 E173 I180 I183 H120 M150 E165 I172 I175 MOAD: Ki=0.183uM
Gene Ontology
Molecular Function
GO:0004462 lactoylglutathione lyase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006749 glutathione metabolic process
GO:0009438 methylglyoxal metabolic process
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
GO:0030316 osteoclast differentiation
GO:0043066 negative regulation of apoptotic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Cellular Component
External links
PDB RCSB:4x2a, PDBe:4x2a, PDBj:4x2a
PDBsum4x2a
PubMed26268338
UniProtQ9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)

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