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3IFE

1.55 Angstrom Resolution Crystal Structure of Peptidase T (pepT-1) from Bacillus anthracis str. 'Ames Ancestor'.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006518biological_processpeptide metabolic process
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0043171biological_processpeptide catabolic process
A0045148molecular_functiontripeptide aminopeptidase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00758
Number of Residues10
DetailsARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. IGFLAHlDTA
ChainResidueDetails
AILE74-ALA83

site_idPS00759
Number of Residues40
DetailsARGE_DAPE_CPG2_2 ArgE / dapE / ACY1 / CPG2 / yscS family signature 2. GADdKAg.LteImvamnylihnpqikhgkIrVAFtpDEEiG
ChainResidueDetails
AGLY140-GLY179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00550
ChainResidueDetails
AASP81

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00550
ChainResidueDetails
AGLU176

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00550
ChainResidueDetails
AHIS79
AASP142
AGLU177
AASP199
AHIS381

219140

PDB entries from 2024-05-01

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