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4WMK

Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with manganese, product ligand and UDP (Product complex II)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
D0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
DCYS62-CYS73

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCpfGfeGKnC
ChainResidueDetails
DCYS71-CYS82

site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCpfGFegkn....C
ChainResidueDetails
DCYS71-CYS82

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC
ChainResidueDetails
DASP47-CYS71

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsRegion: {"description":"Interaction with target proteins","evidences":[{"source":"PubMed","id":"26414444","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26414444","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WNH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26414444","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WLZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WN2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WNH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26414444","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4WM0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4WNH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7606779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EDM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6688526","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1996","firstPage":"50","lastPage":"50","publisher":"Annecy","bookName":"Proceedings of XIth international conference on methods in protein structure analysis","title":"Partial phosphorylation of serine-68 in EGF-1 of human factor IX.","authors":["Harris R.J.","Papac D.I.","Truong L.","Smith K.J."]}}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) serine","featureId":"CAR_000009","evidences":[{"source":"PubMed","id":"2129367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2511201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc...) serine","featureId":"CAR_000010","evidences":[{"source":"PubMed","id":"1517205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

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