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

3R2W

Crystal Structure of UDP-glucose Pyrophosphorylase of Homo Sapiens

Functional Information from GO Data
ChainGOidnamespacecontents
A0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005977biological_processglycogen metabolic process
A0005978biological_processglycogen biosynthetic process
A0006011biological_processUDP-alpha-D-glucose metabolic process
A0007420biological_processbrain development
A0016740molecular_functiontransferase activity
A0016779molecular_functionnucleotidyltransferase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051748molecular_functionUTP-monosaccharide-1-phosphate uridylyltransferase activity
A0070062cellular_componentextracellular exosome
A0070569molecular_functionuridylyltransferase activity
B0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005977biological_processglycogen metabolic process
B0005978biological_processglycogen biosynthetic process
B0006011biological_processUDP-alpha-D-glucose metabolic process
B0007420biological_processbrain development
B0016740molecular_functiontransferase activity
B0016779molecular_functionnucleotidyltransferase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051748molecular_functionUTP-monosaccharide-1-phosphate uridylyltransferase activity
B0070062cellular_componentextracellular exosome
B0070569molecular_functionuridylyltransferase activity
C0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005977biological_processglycogen metabolic process
C0005978biological_processglycogen biosynthetic process
C0006011biological_processUDP-alpha-D-glucose metabolic process
C0007420biological_processbrain development
C0016740molecular_functiontransferase activity
C0016779molecular_functionnucleotidyltransferase activity
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051748molecular_functionUTP-monosaccharide-1-phosphate uridylyltransferase activity
C0070062cellular_componentextracellular exosome
C0070569molecular_functionuridylyltransferase activity
D0003983molecular_functionUTP:glucose-1-phosphate uridylyltransferase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005977biological_processglycogen metabolic process
D0005978biological_processglycogen biosynthetic process
D0006011biological_processUDP-alpha-D-glucose metabolic process
D0007420biological_processbrain development
D0016740molecular_functiontransferase activity
D0016779molecular_functionnucleotidyltransferase activity
D0042802molecular_functionidentical protein binding
D0046872molecular_functionmetal ion binding
D0051748molecular_functionUTP-monosaccharide-1-phosphate uridylyltransferase activity
D0070062cellular_componentextracellular exosome
D0070569molecular_functionuridylyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues204
DetailsRegion: {"description":"Oligomerization"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsRegion: {"description":"Critical for end-to-end subunit interaction"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9M9P3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25860585","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R7P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon