Structure of PDB 4otu Chain B

Receptor sequence
>4otuB (length=182) Species: 279010 (Bacillus licheniformis DSM 13 = ATCC 14580) [Search protein sequence]
TTHFTVTDQWGNVVSYTTTIEQLFGTGILVPGYGLFLNNELTDFDAIPGG
ANEVQPNKRPLSSMTPTIVFKDEKPVLTVGSPGGTTIIASVFQTILNYFE
YGMSLQDAIEEPRIYTNSLTSYRYESGMPEDVRRKLNDFGHKFGSNPVDI
GNVQSIFIDRENKTFMGVADSSRNGTAVGVNI
3D structure
PDB4otu Low resolution X-ray structure of gamma-glutamyltranspeptidase from Bacillus licheniformis: Opened active site cleft and a cluster of acid residues potentially involved in the recognition of a metal ion.
ChainB
Resolution3.022 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 MG B E523 D568 E125 D170
BS02 GLU B T399 T417 E419 D441 S460 S461 M462 G482 T1 T19 E21 D43 S62 S63 M64 G84
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:4otu, PDBe:4otu, PDBj:4otu
PDBsum4otu
PubMed24780583
UniProtQ65KZ6

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