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1GA1

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH A FRAGMENT OF IODOTYROSTATIN (THIS ENZYME RENAMED "SEDOLISIN" IN 2003)

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 374
ChainResidue
AASP328
AVAL329
AGLY344
AGLY346
AASP348
AHOH401

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CL A 375
ChainResidue
ASER245
AARG299
AHOH417
AHOH440
APRO14
ASER20
AGLY93

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 391
ChainResidue
AASN9
APHE48
AASN52
ATHR186
ATYR275
AHOH434
AHOH489
AHOH515

Functional Information from PROSITE/UniProt
site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSlAsPiFVG
ChainResidueDetails
AGLY285-GLY295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsPropeptide: {"description":"Removed in mature form","featureId":"PRO_0000027364","evidences":[{"source":"PubMed","id":"8576087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues364
DetailsDomain: {"description":"Peptidase S53","evidences":[{"source":"PROSITE-ProRule","id":"PRU01032","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues19
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11323721","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"11747435","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11323721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11747435","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GA4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GA6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NLU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M8W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M8Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6M9F","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1nlu
ChainResidueDetails
AGLU80
AASP170
ASER287
AASP84

site_idMCSA1
Number of Residues4
DetailsM-CSA 380
ChainResidueDetails
AGLU80proton shuttle (general acid/base)
AASP84proton shuttle (general acid/base)
AASP170electrostatic stabiliser
ASER287covalent catalysis

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PDB entries from 2025-07-23

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