3RMW
Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant complexed with manganese and UDP-glucose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016757 | molecular_function | glycosyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE UPG A 263 |
Chain | Residue |
A | LEU9 |
A | ASN133 |
A | SER134 |
A | GLY135 |
A | ASP160 |
A | GLY162 |
A | ASP163 |
A | GLN164 |
A | HIS212 |
A | LEU214 |
A | GLY215 |
A | THR10 |
A | LYS218 |
A | MN264 |
A | EDO270 |
A | HOH309 |
A | HOH343 |
A | HOH352 |
A | HOH399 |
A | HOH400 |
A | HOH404 |
A | HOH405 |
A | THR11 |
A | HOH461 |
A | HOH466 |
A | ASN12 |
A | TYR15 |
A | LYS86 |
A | ASP102 |
A | ALA103 |
A | ASP104 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MN A 264 |
Chain | Residue |
A | ASP102 |
A | ASP104 |
A | HIS212 |
A | UPG263 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 265 |
Chain | Residue |
A | ASP3 |
A | GLN94 |
A | HIS151 |
A | GLU155 |
A | HOH417 |
A | HOH418 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 266 |
Chain | Residue |
A | VAL61 |
A | HIS88 |
A | SER91 |
A | LEU92 |
A | HOH340 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 267 |
Chain | Residue |
A | THR93 |
A | VAL143 |
A | HOH293 |
A | HOH446 |
A | HOH447 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 268 |
Chain | Residue |
A | PRO124 |
A | PRO129 |
A | PRO129 |
A | ASP130 |
A | HIS182 |
A | HIS182 |
A | HOH348 |
A | HOH348 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 269 |
Chain | Residue |
A | GLU119 |
A | LEU120 |
A | SER173 |
A | TRP174 |
A | LYS181 |
A | HOH312 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 270 |
Chain | Residue |
A | VAL82 |
A | LYS86 |
A | GLY161 |
A | ASP163 |
A | UPG263 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 271 |
Chain | Residue |
A | THR2 |
A | GLN94 |
A | GLN148 |
A | HIS151 |
A | HOH334 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 272 |
Chain | Residue |
A | PHE170 |
A | PHE171 |
A | HOH283 |
A | HOH356 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 273 |
Chain | Residue |
A | ASP56 |
A | GLU57 |
A | VAL58 |
A | HOH436 |
A | HOH438 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 274 |
Chain | Residue |
A | PRO41 |
A | ASP62 |
A | GLN262 |
A | HOH336 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 275 |
Chain | Residue |
A | ASP45 |
A | LYS49 |
A | GLU52 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 276 |
Chain | Residue |
A | ASP65 |
A | SER66 |
A | HOH371 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 277 |
Chain | Residue |
A | ASP56 |
A | GLU144 |
A | HOH439 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O |
Chain | Residue | Details |
A | LEU9 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ARG77 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ASP102 | |
A | ASP104 | |
A | HIS212 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22160680, ECO:0007744|PDB:3RMW, ECO:0007744|PDB:3T7O |
Chain | Residue | Details |
A | ASN133 | |
A | ASP160 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000250|UniProtKB:P13280 |
Chain | Residue | Details |
A | LYS86 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P13280 |
Chain | Residue | Details |
A | SER44 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:22160680, ECO:0000269|PubMed:30356213, ECO:0007744|PDB:3U2U, ECO:0007744|PDB:3U2V |
Chain | Residue | Details |
A | TYR195 |