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4CFY

SAVINASE CRYSTAL STRUCTURES FOR COMBINED SINGLE CRYSTAL DIFFRACTION AND POWDER DIFFRACTION ANALYSIS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0030435biological_processsporulation resulting in formation of a cellular spore
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLN2
AASP40
ALEU73
AASN75
AILE77
AVAL79

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 302
ChainResidue
AHOH2255
AHOH2264
AALA163
ATYR165
AALA168

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues11
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIst.H
ChainResidueDetails
AVAL28-HIS38

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtIAA
ChainResidueDetails
AHIS62-ALA72

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
ChainResidueDetails
AGLY213-GLY223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues263
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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