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 | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22160680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3RMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22160680","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3RMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3T7O","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13280","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
