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1CSO

CRYSTAL STRUCTURE OF THE OMTKY3 P1 VARIANT OMTKY3-ILE18I IN COMPLEX WITH SGPB

Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAGHC
ChainResidueDetails
ELEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CAepGDSGGPLY
ChainResidueDetails
ECYS191-TYR200

site_idPS00282
Number of Residues23
DetailsKAZAL_1 Kazal serine protease inhibitors family signature. CtieyRplCgSdnktYgnkCnf.C
ChainResidueDetails
ICYS16-CYS38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin
ChainResidueDetails
IILE18
EASP102
ESER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
IASN45

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57
ESER214

site_idMCSA1
Number of Residues5
DetailsM-CSA 608
ChainResidueDetails
EHIS57proton acceptor, proton donor
EASP102electrostatic stabiliser
EGLY193electrostatic stabiliser
ESER195nucleofuge, nucleophile, proton acceptor, proton donor
ESER214electrostatic stabiliser

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PDB entries from 2024-11-06

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