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1NY2

Human alpha thrombin inhibited by RPPGF and hirugen

Functional Information from GO Data
ChainGOidnamespacecontents
10004252molecular_functionserine-type endopeptidase activity
10005576cellular_componentextracellular region
10006508biological_processproteolysis
10007596biological_processblood coagulation
20004252molecular_functionserine-type endopeptidase activity
20005509molecular_functioncalcium ion binding
20006508biological_processproteolysis
20007596biological_processblood coagulation
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR CHAIN 3 OF HIRUGEN
ChainResidue
2PHE34
2ASN98
2ASP100
2ARG175
3HOH423
3HOH429
2LYS36
2LEU65
2ARG67
2ARG73
2THR74
2TYR76
2ILE82
2GLU97

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
2LEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
2ASP189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues254
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"4-hydroxyproline; partial","evidences":[{"source":"PubMed","id":"3182782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3366244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2ASP102
2HIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2SER195
2GLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2SER195
2GLY193

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2ASP102
2SER195
2GLY193
2HIS57

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2ASP102
2SER195
2HIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
2ASP102
2SER195
2HIS57
2GLY196

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PDB entries from 2025-10-22

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