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3RMW

Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant complexed with manganese and UDP-glucose

Functional Information from GO Data
ChainGOidnamespacecontents
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE UPG A 263
ChainResidue
ALEU9
AASN133
ASER134
AGLY135
AASP160
AGLY162
AASP163
AGLN164
AHIS212
ALEU214
AGLY215
ATHR10
ALYS218
AMN264
AEDO270
AHOH309
AHOH343
AHOH352
AHOH399
AHOH400
AHOH404
AHOH405
ATHR11
AHOH461
AHOH466
AASN12
ATYR15
ALYS86
AASP102
AALA103
AASP104

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MN A 264
ChainResidue
AASP102
AASP104
AHIS212
AUPG263

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 265
ChainResidue
AASP3
AGLN94
AHIS151
AGLU155
AHOH417
AHOH418

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 266
ChainResidue
AVAL61
AHIS88
ASER91
ALEU92
AHOH340

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 267
ChainResidue
ATHR93
AVAL143
AHOH293
AHOH446
AHOH447

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 268
ChainResidue
APRO124
APRO129
APRO129
AASP130
AHIS182
AHIS182
AHOH348
AHOH348

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 269
ChainResidue
AGLU119
ALEU120
ASER173
ATRP174
ALYS181
AHOH312

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 270
ChainResidue
AVAL82
ALYS86
AGLY161
AASP163
AUPG263

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 271
ChainResidue
ATHR2
AGLN94
AGLN148
AHIS151
AHOH334

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 272
ChainResidue
APHE170
APHE171
AHOH283
AHOH356

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 273
ChainResidue
AASP56
AGLU57
AVAL58
AHOH436
AHOH438

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 274
ChainResidue
APRO41
AASP62
AGLN262
AHOH336

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 275
ChainResidue
AASP45
ALYS49
AGLU52

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 276
ChainResidue
AASP65
ASER66
AHOH371

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 277
ChainResidue
AASP56
AGLU144
AHOH439

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
ALEU9

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X
ChainResidueDetails
AARG77

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3QVB, ECO:0007744|PDB:3RMV, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7M, ECO:0007744|PDB:3T7N, ECO:0007744|PDB:3T7O, ECO:0007744|PDB:3U2T, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V, ECO:0007744|PDB:3U2W, ECO:0007744|PDB:3U2X
ChainResidueDetails
AASP102
AASP104
AHIS212

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O
ChainResidueDetails
AASN133
AASP160

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
ATYR195

218853

PDB entries from 2024-04-24

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