3QVB
Crystal Structure of Human Glycogenin-1 (GYG1) complexed with manganese and UDP
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 | 4 |
Details | BINDING SITE FOR RESIDUE MN A 263 |
Chain | Residue |
A | ASP102 |
A | ASP104 |
A | HIS212 |
A | UDP264 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE UDP A 264 |
Chain | Residue |
A | ASP102 |
A | ALA103 |
A | ASP104 |
A | HIS212 |
A | LEU214 |
A | GLY215 |
A | LYS218 |
A | MN263 |
A | HOH388 |
A | LEU9 |
A | THR10 |
A | THR11 |
A | TYR15 |
A | VAL82 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 265 |
Chain | Residue |
A | HIS29 |
A | ARG30 |
A | ASN110 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 266 |
Chain | Residue |
A | THR93 |
A | SER142 |
A | VAL143 |
A | GLU144 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 267 |
Chain | Residue |
A | GLU119 |
A | LEU120 |
A | SER173 |
A | LYS181 |
A | HOH364 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 268 |
Chain | Residue |
A | HIS88 |
A | LEU92 |
A | HOH308 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 269 |
Chain | Residue |
A | SER44 |
A | ASP45 |
A | SER46 |
A | SER158 |
A | PHE159 |
A | ASP160 |
A | GLY161 |
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 | PHE195 |