Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5KY2

mouse POFUT1 in complex with O-glucosylated mouse Factor VII EGF1 and GDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0001756biological_processsomitogenesis
A0005783cellular_componentendoplasmic reticulum
A0006004biological_processfucose metabolic process
A0006486biological_processobsolete protein glycosylation
A0007219biological_processNotch signaling pathway
A0007399biological_processnervous system development
A0007507biological_processheart development
A0008417molecular_functionfucosyltransferase activity
A0008593biological_processregulation of Notch signaling pathway
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0036066biological_processprotein O-linked glycosylation via fucose
A0046922molecular_functionpeptide-O-fucosyltransferase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CqDhlksYvCfC
ChainResidueDetails
BCYS102-CYS113

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CfCllDfeGRnC
ChainResidueDetails
BCYS111-CYS122

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCasnp..........Cqnggt..CqDhlksYvC
ChainResidueDetails
BASP87-CYS111

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9H488","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Xyl...) serine; alternate","evidences":[{"source":"UniProtKB","id":"P08709","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon