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1GCI

THE 0.78 ANGSTROMS STRUCTURE OF A SERINE PROTEASE-BACILLUS LENTUS SUBTILISIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 276
ChainResidue
AVAL104
ASER132
AALA133
ATHR134
AHOH1004
AHOH1007
AHOH1129

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 277
ChainResidue
ALEU75
AASN77
AILE79
AVAL81
AGLN2
AASP41

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 278
ChainResidue
AALA169
ATYR171
AALA174
AGLY195
AASP197
AHOH1112

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
APHE50
ATRP113
APRO239
AHOH1070
AHOH1077
AHOH1092
AHOH1096
AHOH1166
AHOH1167
AHOH1168
AHOH1175

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIst.H
ChainResidueDetails
AVAL28-HIS39

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

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
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:
ChainResidueDetails
AGLN2
AASP41
ALEU75
AASN77
AILE79
AVAL81
AALA169
ATYR171
AALA174

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

223532

PDB entries from 2024-08-07

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