3RMV
Crystal Structure of Human Glycogenin-1 (GYG1) T83M mutant 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 | 16 |
| Details | BINDING SITE FOR RESIDUE UDP A 264 |
| Chain | Residue |
| A | ASP102 |
| A | ALA103 |
| A | ASP104 |
| A | HIS212 |
| A | GLY215 |
| A | LYS218 |
| A | MN263 |
| A | HOH424 |
| A | HOH426 |
| A | HOH451 |
| A | HOH482 |
| A | LEU9 |
| A | THR10 |
| A | THR11 |
| A | ASN12 |
| A | TYR15 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 265 |
| Chain | Residue |
| A | GLU119 |
| A | LEU120 |
| A | PHE171 |
| A | SER173 |
| A | TRP174 |
| A | LYS181 |
| A | HOH268 |
| A | HOH311 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 266 |
| Chain | Residue |
| A | ASP178 |
| A | ASP178 |
| A | ILE179 |
| A | ILE179 |
| A | HOH483 |
| A | HOH483 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 267 |
| Chain | Residue |
| A | ASP3 |
| A | GLN94 |
| A | HIS151 |
| A | GLU155 |
| A | HOH469 |
| A | HOH472 |
| A | HOH473 |
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 |
