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1GA4

CRYSTAL STRUCTURE ANALYSIS OF PSCP (PSEUDOMONAS SERINE-CARBOXYL PROTEINASE) COMPLEXED WITH INHIBITOR PSEUDOIODOTYROSTATIN (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 Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 391
ChainResidue
ATHR186
ATYR275
ALEU280
AHOH434
AHOH489
AHOH564
AASN9
APHE48
AASN52

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR CHAIN I OF PSEUDOIODOTYROSTATIN
ChainResidue
AILE35
AASP74
AGLY77
AGLU80
ATRP81
ASER133
ALEU134
AGLY135
ATRP136
ASER167
AGLY169
AASP170
AGLU171
AGLU175
AARG179
ASER190
AGLY285
ATHR286
ASER287
AHOH637

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 Residues3
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:10488127
ChainResidueDetails
AGLU80
AASP84
ASER287

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AASP328
AVAL329
AGLY344
AGLY346
AASP348

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 2024-09-18

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