Structure of PDB 2dbx Chain D

Receptor sequence
>2dbxD (length=190) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TTHYSVVDKDGNAVAVTYTLNTTFGTGIVAGESGILLNNQMDDFSAKPGV
PNVYGLVGGDANAVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITT
VLQMVVNSIDYGLNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAK
GQKVALKEAMGSTQSIMVGPDGELYGASDPRSVDDLTAGY
3D structure
PDB2dbx Crystal structures of gamma-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate.
ChainD
Resolution1.7 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 CA D D569 P570 S572 D575 D179 P180 S182 D185
BS02 GLU D T391 N411 D433 Y444 S462 S463 G483 G484 T1 N21 D43 Y54 S72 S73 G93 G94
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:2dbx, PDBe:2dbx, PDBj:2dbx
PDBsum2dbx
PubMed16618936
UniProtP18956|GGT_ECOLI Glutathione hydrolase proenzyme (Gene Name=ggt)

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