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4SGA

STRUCTURES OF PRODUCT AND INHIBITOR COMPLEXES OF STREPTOMYCES GRISEUS PROTEASE A AT 1.8 ANGSTROMS RESOLUTION. A MODEL FOR SERINE PROTEASE CATALYSIS

Functional Information from GO Data
ChainGOidnamespacecontents
E0004252molecular_functionserine-type endopeptidase activity
E0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR CHAIN P OF TETRAPEPTIDE ACE-PRO-ALA-PRO-PHE
ChainResidue
EHIS57
ESER195
ESER214
EGLY215
EGLY216
EHOH391
PHOH356
PHOH357
EVAL169
EASN170
ETYR171
EALA192
EGLN192
EPRO192
EGLY193
EASP194

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. CAqpGDSGGSLF
ChainResidueDetails
ECYS191-PHE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
EHIS57
EASP102
ESER195

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57
ESER214

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
EASP102
ESER195
EGLY193
EHIS57

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PDB entries from 2024-11-06

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