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1SUB

CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN

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 295
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 297
ChainResidue
AGLY169
ATYR171
AVAL174
AGLU195
AASP197
AHOH444

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACN A 298
ChainResidue
ASER37
APHE58
AARG186

site_idACT
Number of Residues3
DetailsACTIVE SITE, THE CATALYTIC TRIAD
ChainResidue
AASP32
AHIS64
ACSD221

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. HGThVAGtVAA
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:5249818
ChainResidueDetails
AASP32
AHIS64
ACSD221

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AGLN2
AASP41
AASN77
AILE79
AVAL81
AGLY169
ATYR171
AVAL174
ALEU75

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 723
ChainResidueDetails
AASP32electrostatic interaction, electrostatic stabiliser
AHIS64proton acceptor, proton donor
AASN155electrostatic interaction, electrostatic stabiliser
ACSD221nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-04-17

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