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4SGB

STRUCTURE OF THE COMPLEX OF STREPTOMYCES GRISEUS PROTEINASE B AND POLYPEPTIDE CHYMOTRYPSIN INHIBITOR-1 FROM RUSSET BURBANK POTATO TUBERS AT 2.1 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 E 244
ChainResidue
EASN67
ESER68
EALA69
EHOH304
EHOH312

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 E 245
ChainResidue
EARG139
EGLY156
ETHR157
EHOH252

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA E 8
ChainResidue
EGLY120
EASP120
EILE121
ETYR243
EHOH250
IARG51

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
ECYS189-TYR200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reactive bond for chymotrypsin","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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

251422

PDB entries from 2026-04-01

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