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3FNM

Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis

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 AVN B 1
ChainResidue
AARG103
BMET453
BGLY472
BGLY473
BILE476
BHOH579
BTHR380
BTHR398
BASN400
BGLU419
BASP422
BTYR433
BSER451
BSER452

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AVN D 1
ChainResidue
CARG103
DHOH27
DTHR380
DTHR398
DASN400
DGLU419
DASP422
DTYR433
DSER451
DSER452
DMET453
DGLY472
DGLY473
DILE476

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGGGGFAVIHlAngenvaldfrek......APLK
ChainResidueDetails
AILE82-LYS109

site_idPS00462
Number of Residues25
DetailsG_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHySVadrwGNaVSvTyTINasYG
ChainResidueDetails
BTHR380-GLY404

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PDB entries from 2024-07-24

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