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

5UW4

Activated yeast Glycogen Synthase in complex with UDP glucosamine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004373molecular_functionglycogen (starch) synthase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005978biological_processglycogen biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0042802molecular_functionidentical protein binding
A0140678molecular_functionmolecular function inhibitor activity
B0004373molecular_functionglycogen (starch) synthase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005978biological_processglycogen biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0042802molecular_functionidentical protein binding
B0140678molecular_functionmolecular function inhibitor activity
C0004373molecular_functionglycogen (starch) synthase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005978biological_processglycogen biosynthetic process
C0016757molecular_functionglycosyltransferase activity
C0042802molecular_functionidentical protein binding
C0140678molecular_functionmolecular function inhibitor activity
D0004373molecular_functionglycogen (starch) synthase activity
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005978biological_processglycogen biosynthetic process
D0016757molecular_functionglycosyltransferase activity
D0042802molecular_functionidentical protein binding
D0140678molecular_functionmolecular function inhibitor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CARG20
BARG20
AARG20
DARG20

site_idSWS_FT_FI2
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000255
ChainResidueDetails
CSER159
CSER363
BSER159
BSER363
ASER159
ASER363
DSER159
DSER363

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
CSER467
BSER467
ASER467
DSER467

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
CSER651
BSER651
ASER651
DSER651

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PHO85 => ECO:0000269|PubMed:9584169, ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956
ChainResidueDetails
CSER655
BSER655
ASER655
DSER655

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
CSER661
CSER663
BSER661
BSER663
ASER661
ASER663
DSER661
DSER663

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by PHO85 => ECO:0000269|PubMed:9584169
ChainResidueDetails
CTHR668
BTHR668
ATHR668
DTHR668

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon