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1EKB

THE SERINE PROTEASE DOMAIN OF ENTEROPEPTIDASE BOUND TO INHIBITOR VAL-ASP-ASP-ASP-ASP-LYS-CHLOROMETHANE

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 310
ChainResidue
BGLU24
BHIS71
BGLU126

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 311
ChainResidue
BASP50
BGLU185
BHIS243
BHOH479

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR CHAIN C OF VAL-ASP-ASP-ASP-ASP-LYK PEPTIDE
ChainResidue
BTYR174
BASP189
BSER190
BGLN192
BGLY193
BSER195
BSER214
BPHE215
BGLY216
BGLY226
BHOH407
BHOH438
CHOH436
CHOH445
CHOH521
BHIS57
BLYS99

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLM
ChainResidueDetails
BASP189-MET200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:10493881
ChainResidueDetails
BHIS57
BASP102
BSER195

site_idSWS_FT_FI2
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN75
BASN113
BASN175

221051

PDB entries from 2024-06-12

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