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1SEL

CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION

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 276
ChainResidue
AGLN2
AASP41
ALEU75
AASN77
ATHR79
AVAL81

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 277
ChainResidue
AHOH325
AHOH326
AALA169
ATYR171
AVAL174

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 276
ChainResidue
BGLN2
BASP41
BLEU75
BASN77
BTHR79
BVAL81

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 277
ChainResidue
BALA169
BLYS170
BTYR171
BVAL174
BHOH286

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP32
AHIS64
ASE7221
BASP32
BHIS64
BSE7221

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:8512925
ChainResidueDetails
AGLN2
BGLN2
BASP41
BLEU75
BASN77
BTHR79
BVAL81
BALA169
BTYR171
BVAL174
AASP41
ALEU75
AASN77
ATHR79
AVAL81
AALA169
ATYR171
AVAL174

225681

PDB entries from 2024-10-02

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