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1BFK

CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 276
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
ATHR79
AVAL81

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CCN A 354
ChainResidue
AHIS64
AASN155
ASER221
ACCN355
ACCN357

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CCN A 355
ChainResidue
AHIS64
ASER125
ALEU126
ACCN354

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CCN A 356
ChainResidue
ASER99
ALYS265

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CCN A 357
ChainResidue
ASER125
AALA152
AGLY154
ASER221
ACCN354

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CCN A 358
ChainResidue
AGLN36
ATHR59
AASP60
AHOH339

site_idACT
Number of Residues3
Details
ChainResidue
AASP32
AHIS64
ASER221

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
ASER221

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
ASER221
AHIS64
AASP32

237735

PDB entries from 2025-06-18

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