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1C1V

RECRUITING ZINC TO MEDIATE POTENT, SPECIFIC INHIBITION OF SERINE PROTEASES

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN H 254
ChainResidue
HHIS57
HSER201
HBAB410

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ZN H 255
ChainResidue
HBAB410
HHOH546

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA H 409
ChainResidue
HHOH452
HHOH454
HARG227
HLYS230
HHOH428
HHOH431

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE BAB H 410
ChainResidue
HLEU41
HLYS60
HASP195
HALA196
HGLU198
HSER201
HVAL219
HTRP221
HGLY222
HGLY225
HZN254
HZN255
HHOH545

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR CHAIN I OF PROTEIN (ACETYL HIRUDIN)
ChainResidue
HPHE34
HLYS36
HGLN38
HLEU40
HLEU65
HARG73
HTHR74
HARG75
HTYR76
HLYS81
HILE82
HMET84
IHOH499
IHOH597
IHOH790

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
HASP195-VAL206

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI3
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

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HSER201
HGLY202

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HGLY199
HSER201

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HGLY199
HASP102
HSER201
HHIS57

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER201
HHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HSER201
HHIS57
HGLY202

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PDB entries from 2025-07-30

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