Structure of PDB 2e0x Chain B

Receptor sequence
>2e0xB (length=178) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
TTHYSVVDKDGNAVAVTYTLNTTFGTGIVAGESGILLNNQMDDFSAKDAN
AVGPNKRPLSSMSPTIVVKDGKTWLVTGSPGGSRIITTVLQMVVNSIDYG
LNVAEATNAPRFHHQWLPDELRVEKGFSPDTLKLLEAKGQKVALKEAMGS
TQSIMVGPDGELYGASDPRSVDDLTAGY
3D structure
PDB2e0x Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism
ChainB
Resolution1.95 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 B D569 P570 S572 D575 D167 P168 S170 D173
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:2e0x, PDBe:2e0x, PDBj:2e0x
PDBsum2e0x
PubMed17135273
UniProtP18956|GGT_ECOLI Glutathione hydrolase proenzyme (Gene Name=ggt)

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