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1AVT

SUBTILISIN CARLSBERG D-PARA-CHLOROPHENYL-1-ACETAMIDO BORONIC ACID INHIBITOR COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 300
ChainResidue
AALA169
ATYR171
AVAL174
AHOH356
AHOH357

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 301
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
ATHR79
AVAL81

site_idACT
Number of Residues3
DetailsSERINE OF THE ACTIVE SITE HAS BEEN CHEMICALLY MODIFIED TO INCLUDE A COVALENT BOND FROM OG TO BORON OF THE INHIBITOR.
ChainResidue
AASP32
AHIS64
ACLD221

site_idM1
Number of Residues4
DetailsCALCIUM METAL BINDING SITE 1.
ChainResidue
ALEU75
AASN77
ATHR79
AVAL81

site_idM2
Number of Residues2
DetailsCALCIUM METAL BINDING SITE 2.
ChainResidue
AALA169
AVAL174

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH
ChainResidueDetails
AVAL28-HIS39

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA
ChainResidueDetails
AHIS64-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8512925","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
ACLD221
AHIS64
AASP32

238895

PDB entries from 2025-07-16

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