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5UBM

Crystal structure of human C1s in complex with inhibitor gigastasin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
I0004857molecular_functionenzyme inhibitor activity
I0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CeCrnQvcGRgC
ChainResidueDetails
ICYS28-CYS39

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGAFA
ChainResidueDetails
AASP626-ALA637

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"10775260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues66
DetailsDomain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12788922","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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