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3U2V

Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese, UDP and maltohexaose

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
ALEU9
ALYS218
BLEU9
BTHR11
BTYR15
BASP102
BASP104
BASN133
BASP163
BGLN164
BGLY215
ATHR11
BLYS218
ATYR15
AASP102
AASP104
AASN133
AASP163
AGLN164
AGLY215

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
AASN12
AHIS212
BASN12
BHIS212

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7O
ChainResidueDetails
AARG77
ALYS86
ASER134
AASP160
BARG77
BLYS86
BSER134
BASP160

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
AALA103
BALA103

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ALYS86
BLYS86

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2
BTHR2

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ASER44
BSER44

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V
ChainResidueDetails
ATYR195
BTYR195

238268

PDB entries from 2025-07-02

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