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1ELV

CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idCAT
Number of Residues3
DetailsTHE CATALYTIC TRIAD IS: HIS A460 (57), ASP A514 (102), SER A617 (195) (RESIDUE NUMBERS IN THE REFERENCE CHYMOTRYPSINOGEN MOLECULE).
ChainResidue
AHIS460
AASP514
ASER617

Functional Information from PROSITE/UniProt
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGAFA
ChainResidueDetails
AASP611-ALA622

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system
ChainResidueDetails
AHIS460
AASP514
ASER617

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12788922, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN391

219140

PDB entries from 2024-05-01

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