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3USQ

Structure of D159S/Y194F glycogenin mutant truncated at residue 270

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 271
ChainResidue
AHIS28
AASN109

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 272
ChainResidue
AHOH312
AGLU117
AGLU118
ALEU119
APHE170
ASER172
ALYS180
AHOH294

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 273
ChainResidue
AILE178
AHOH275

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
ASER159

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
AASP103
AHIS211
AASP101

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
APHE194

221051

PDB entries from 2024-06-12

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