Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4WM0

Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with acceptor ligand

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 Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM
ChainResidueDetails
DASP64
DASP65
DGLY48
DGLN50
DASP47

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6688526
ChainResidueDetails
AHIS382
DASP64
AASP227

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|Ref.28
ChainResidueDetails
DSER68
AASN384

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591
ChainResidueDetails
DSER53

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:1517205, ECO:0000269|PubMed:25456591
ChainResidueDetails
DSER61

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon