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1AV7

SUBTILISIN CARLSBERG L-NAPHTHYL-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 Residues3
DetailsBINDING SITE FOR RESIDUE NA A 300
ChainResidue
AALA169
ATYR171
AVAL174

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
ASBL221

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

site_idM2
Number of Residues2
DetailsSODIUM 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

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
AGLY219-GLY229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP32
AHIS64
ASBL221

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:8512925
ChainResidueDetails
AASN77
ATHR79
AVAL81
AALA169
ATYR171
AVAL174
AGLN2
AASP41
ALEU75

221051

PDB entries from 2024-06-12

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