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1YCP

THE CRYSTAL STRUCTURE OF FIBRINOGEN-AA PEPTIDE 1-23 (F8Y) BOUND TO BOVINE THROMBIN EXPLAINS WHY THE MUTATION OF PHE-8 TO TYROSINE STRONGLY INHIBITS NORMAL CLEAVAGE AT ARGININE-16

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
J0004252molecular_functionserine-type endopeptidase activity
J0005576cellular_componentextracellular region
J0006508biological_processproteolysis
J0007596biological_processblood coagulation
K0004252molecular_functionserine-type endopeptidase activity
K0005509molecular_functioncalcium ion binding
K0006508biological_processproteolysis
K0007596biological_processblood coagulation
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
M0004252molecular_functionserine-type endopeptidase activity
M0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR CHAIN F OF FIBRINOPEPTIDE A-ALPHA
ChainResidue
FHOH450
HGLU97
HLEU99
HILE174
HASP189
HALA190
HCYS191
HGLU192
HGLY193
HSER195
HSER214
FHOH481
HTRP215
HGLY216
HGLY219
HHOH411
FHOH482
FHOH668
HLEU41
HHIS57
HTYR60
HTRP96
HLYS97

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR CHAIN N OF FIBRINOPEPTIDE A-ALPHA
ChainResidue
HTRP60
HHOH504
KHIS57
KLYS97
KGLU97
KHOH442
KHOH495
MILE174
MASP189
MGLU192
MGLY193
MSER195
MSER214
MTRP215
MGLY216
MGLY219

Functional Information from PROSITE/UniProt
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
MASP189-VAL200
HASP189-VAL200

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
KLEU53-CYS58
HLEU53-CYS58

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by thrombin; to release fibrinopeptide A
ChainResidueDetails
FARG316
NARG316
HSER195

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16807684
ChainResidueDetails
FSER303
NSER303

218853

PDB entries from 2024-04-24

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