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3QVB

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 263
ChainResidue
AASP102
AASP104
AHIS212
AUDP264

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE UDP A 264
ChainResidue
AASP102
AALA103
AASP104
AHIS212
ALEU214
AGLY215
ALYS218
AMN263
AHOH388
ALEU9
ATHR10
ATHR11
ATYR15
AVAL82

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 265
ChainResidue
AHIS29
AARG30
AASN110

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 266
ChainResidue
ATHR93
ASER142
AVAL143
AGLU144

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 267
ChainResidue
AGLU119
ALEU120
ASER173
ALYS181
AHOH364

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 268
ChainResidue
AHIS88
ALEU92
AHOH308

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 269
ChainResidue
ASER44
AASP45
ASER46
ASER158
APHE159
AASP160
AGLY161

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
ALEU9
ALYS218
ATHR11
ATYR15
AASP102
AASP104
AASN133
AASP163
AGLN164
AGLY215

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
AASN12
AHIS212

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7O
ChainResidueDetails
AARG77
ALYS86
ASER134
AASP160

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
AALA103

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ALYS86

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
ATHR2

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280
ChainResidueDetails
ASER44

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V
ChainResidueDetails
APHE195

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PDB entries from 2025-06-11

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