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3V8Y

Structure of apo-glycogenin truncated at residue 270

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 301
ChainResidue
AHIS28
AALA108
AASN109

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 302
ChainResidue
AASP129
AASN167
AASN171
AHOH409
AHOH431

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 303
ChainResidue
AILE178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91
ChainResidueDetails
ALEU8
AASN132
AASP159

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P46976
ChainResidueDetails
AARG76

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZCT, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V8Z, ECO:0007744|PDB:3V91
ChainResidueDetails
AASP101
AASP103
AHIS211

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:10049511
ChainResidueDetails
ALYS85

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0000250|UniProtKB:P46976
ChainResidueDetails
ATHR1

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA; in vitro => ECO:0000269|PubMed:3151442
ChainResidueDetails
ASER43

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:8143846
ChainResidueDetails
ATYR194

227111

PDB entries from 2024-11-06

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