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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 Residues1
DetailsMOD_RES: 4-hydroxyproline; partial => ECO:0000269|PubMed:3182782, ECO:0000269|PubMed:3366244
ChainResidueDetails
4PRO382
2ASP102
2SER195

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:873923
ChainResidueDetails
2ASN60

218853

PDB entries from 2024-04-24

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