Structure of PDB 6xpc Chain B

Receptor sequence
>6xpcB (length=189) Species: 9606 (Homo sapiens) [Search protein sequence]
TAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSIT
NEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTA
TALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETR
HHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
3D structure
PDB6xpc Crystal structures of glutathione- and inhibitor-bound human GGT1: critical interactions within the cysteinylglycine binding site.
ChainB
Resolution2.26 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.2: gamma-glutamyltransferase.
3.4.19.13: glutathione gamma-glutamate hydrolase.
3.4.19.14: leukotriene-C4 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 GSH B T381 N401 Y403 D423 S451 S452 G473 G474 T1 N21 Y23 D43 S71 S72 G93 G94
Gene Ontology
Molecular Function
GO:0036374 glutathione hydrolase activity
Biological Process
GO:0006751 glutathione catabolic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6xpc, PDBe:6xpc, PDBj:6xpc
PDBsum6xpc
PubMed33187988
UniProtP19440|GGT1_HUMAN Glutathione hydrolase 1 proenzyme (Gene Name=GGT1)

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