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6M3B

hAPC-c25k23 Fab complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
D0005509molecular_functioncalcium ion binding
D0005576cellular_componentextracellular region
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CiDgigsFsCdC
ChainResidueDetails
DCYS69-CYS80

site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EciEEiCdfeeakEifqnvddtla.FW
ChainResidueDetails
DGLU16-TRP41

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CdCrsGweGRfC
ChainResidueDetails
DCYS78-CYS89

site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPMV
ChainResidueDetails
AASP189-VAL200

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH
ChainResidueDetails
BTYR196-HIS202
CTYR205-HIS211

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CdCrsGWegrf....C
ChainResidueDetails
DCYS78-CYS89
DCYS118-CYS133

site_idPS01187
Number of Residues33
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQClvlplehpcaslc.Cghgt...CiDgigsFsC
ChainResidueDetails
DASP46-CYS78

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI2
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_FI3
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_FI4
Number of Residues40
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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