Structure of PDB 3whs Chain B

Receptor sequence
>3whsB (length=183) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence]
TTHFTVADRWGNVVSYTTTIEQLFGTGIMVPDYGVILNNELTDFDAIPGG
ANEVQPNKRPLSSMTPTILFKDDKPVLTVGSPGGATIISSVLQTILYHIE
YGMELKAAVEEPRIYTNSMSSYRYEDGVPKDVLSKLNGMGHKFGTSPVDI
GNVQSISIDHENGTFKGVADSSRNGAAIGINLK
3D structure
PDB3whs Structure of Bacillus subtilis gamma-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue.
ChainB
Resolution1.8 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.
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 AVN B T403 T421 E423 D445 S464 S465 G486 I489 T1 T19 E21 D43 S62 S63 G84 I87
Gene Ontology
Molecular Function
GO:0036374 glutathione hydrolase activity
Biological Process
GO:0006751 glutathione catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3whs, PDBe:3whs, PDBj:3whs
PDBsum3whs
PubMed24531494
UniProtP54422|GGT_BACSU Glutathione hydrolase proenzyme (Gene Name=ggt)

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