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1EQ9

CRYSTAL STRUCTURE OF FIRE ANT CHYMOTRYPSIN COMPLEXED TO PMSF

Functional Information from GO Data
ChainGOidnamespacecontents
A0004175molecular_functionendopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
B0004175molecular_functionendopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016485biological_processprotein processing
B0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PMS A 1201
ChainResidue
AALA190
ACYS191
AHIS192
AGLY193
ASER195
APHE215
AHOH905
AHOH937
AHOH1055

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PMS B 1202
ChainResidue
BHIS357
BALA490
BCYS491
BHIS492
BGLY493
BSER495
BPHE515
BHOH828
BHOH910

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. GAchGDSGGPLV
ChainResidueDetails
AGLY189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues440
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10801356","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA10
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193
AASP95
AHIS57

site_idCSA11
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP395
BGLY493
BSER495
BHIS357

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER495
BHIS357
BASP402

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57
ASER214

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BGLY493
BSER495
BHIS357
BASP402

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BSER495
BHIS357
BGLY496
BASP402

site_idCSA8
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
ASER195
AGLY193
AASP95
AHIS57
ASER214

site_idCSA9
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP395
BGLY493
BSER514
BSER495
BHIS357

246031

PDB entries from 2025-12-10

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