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3WHI

Crystal structure of unautoprocessed form of IS1-inserted Pro-subtilisin E

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AGLN92
AASP131
ALEU165
AASN167
AILE169
AVAL171

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASN167
BILE169
BVAL171
BGLN92
BASP131
BLEU165

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH
ChainResidueDetails
AVAL118-HIS129

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtIAA
ChainResidueDetails
AHIS154-ALA164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:9811547
ChainResidueDetails
AASP122
AHIS154
AALA311
BASP122
BHIS154
BALA311

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:9811547
ChainResidueDetails
AGLN92
AASP287
BGLN92
BASP131
BLEU165
BASN167
BILE169
BVAL171
BALA259
BTYR261
BTHR264
AASP131
BASP287
ALEU165
AASN167
AILE169
AVAL171
AALA259
ATYR261
ATHR264

224201

PDB entries from 2024-08-28

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