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1AUT

Human activated protein C

Functional Information from GO Data
ChainGOidnamespacecontents
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
L0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 0G6 C 1
ChainResidue
CHOH4
CGLY193
CSER195
CSER214
CTRP215
CGLY216
CGLY219
CHOH265
CHIS57
CTHR98
CTHR99
CASN174
CASP189
CALA190
CCYS191
CGLU192

Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiDgigsFsCdC
ChainResidueDetails
LCYS69-CYS80

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CdCrsGweGRfC
ChainResidueDetails
LCYS78-CYS89

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPMV
ChainResidueDetails
CASP189-VAL200

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CdCrsGWegrf....C
ChainResidueDetails
LCYS78-CYS89
LCYS118-CYS133

site_idPS01187
Number of Residues33
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQClvlplehpcaslc.Cghgt...CiDgigsFsC
ChainResidueDetails
LASP46-CYS78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues238
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; atypical; partial","evidences":[{"source":"PubMed","id":"1694179","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"2991887","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CSER195
CGLY196

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CGLY193
CHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57
CGLY196

246704

PDB entries from 2025-12-24

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