Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Z8J

Crystal Structure of Escherichia coli gamma-Glutamyltranspeptidase in Complex with Azaserine prepared in the dark

Functional Information from GO Data
ChainGOidnamespacecontents
A0006751biological_processglutathione catabolic process
A0036374molecular_functionglutathione hydrolase activity
B0006751biological_processglutathione catabolic process
B0036374molecular_functionglutathione hydrolase activity
C0006751biological_processglutathione catabolic process
C0036374molecular_functionglutathione hydrolase activity
D0006751biological_processglutathione catabolic process
D0036374molecular_functionglutathione hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZS B 390
ChainResidue
AARG114
BPRO482
BGLY483
BGLY484
BHOH596
BHOH641
BTHR391
BASN411
BGLN430
BASP433
BTYR444
BSER462
BSER463
BMET464

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AZS D 390
ChainResidue
CARG114
DTHR391
DTHR409
DASN411
DGLN430
DASP433
DTYR444
DSER462
DSER463
DMET464
DGLY483
DGLY484
DHOH586
DHOH608

Functional Information from PROSITE/UniProt
site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHySVvdkdGNaVAvTyTLNttFG
ChainResidueDetails
BTHR391-GLY415

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:16618936, ECO:0000269|PubMed:18555071
ChainResidueDetails
BTHR391
DTHR391

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16618936
ChainResidueDetails
BTHR409
BASN411
BGLN430
BASP433
DTHR409
DASN411
DGLN430
DASP433

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BSER462
BGLY483
DSER462
DGLY483

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon