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1DBI

CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE PROTEASE

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 701
ChainResidue
AASP5
AASP48
AGLU83
AASN86
ATHR88
AILE90

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 702
ChainResidue
AHOH301
AHOH302
AHOH303
ATYR176
AVAL179
AASP202

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 703
ChainResidue
AASP58
AASP63
AASP65
AHOH304
AHOH305
AHOH306

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 704
ChainResidue
APRO47
AASP50
AGLU83
AHOH307
AHOH308
AHOH309

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. IAVIDTGVdytH
ChainResidueDetails
AILE35-HIS46

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGiAAA
ChainResidueDetails
AHIS72-ALA82

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG
ChainResidueDetails
AGLY224-GLY234

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:10588904
ChainResidueDetails
AASP39
AHIS72
ASER226

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:10588904
ChainResidueDetails
AASP5
ATHR88
AILE90
ATYR176
AVAL179
AASP202
APRO47
AASP48
AASP50
AASP58
AASP63
AASP65
AGLU83
AASN86

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
ASER226
AASP39
AHIS72

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PDB entries from 2024-07-17

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