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1SCJ

CRYSTAL STRUCTURE OF SUBTILISIN-PROPEPTIDE 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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 381
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 382
ChainResidue
AALA169
ATYR171
ATHR174
AALA176
AASP197
AHOH401

site_idAVE
Number of Residues3
DetailsACTIVE SITE MUTATION IS SER 221 CYS THAT BLOCKS THE PROTEOLYTIC ACTIVITY.
ChainResidue
ACYS221
AHIS64
AASP32

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

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:9811547
ChainResidueDetails
AHIS64
AASP32
ACYS221

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811547
ChainResidueDetails
AGLN2
AASP41
AASN77
AILE79
AVAL81
AALA169
ATYR171
ATHR174
AASP197
ALEU75

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PDB entries from 2024-06-12

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