4Y9X
Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0006011 | biological_process | UDP-alpha-D-glucose metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0016758 | molecular_function | hexosyltransferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MN A 401 |
| Chain | Residue |
| A | ASP136 |
| A | HIS258 |
| A | UPG404 |
| A | HOH508 |
| A | HOH530 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 402 |
| Chain | Residue |
| A | ARG242 |
| A | LYS319 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue 3PG A 403 |
| Chain | Residue |
| A | ARG185 |
| A | VAL186 |
| A | THR187 |
| A | HIS258 |
| A | ASN260 |
| A | UPG404 |
| A | HOH510 |
| A | HOH560 |
| A | GLY183 |
| A | GLY184 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue UPG A 404 |
| Chain | Residue |
| A | PRO50 |
| A | ALA51 |
| A | LEU52 |
| A | GLU54 |
| A | SER81 |
| A | GLY113 |
| A | LYS114 |
| A | ASP134 |
| A | SER135 |
| A | ASP136 |
| A | LEU209 |
| A | GLY211 |
| A | TYR229 |
| A | GLU232 |
| A | ARG256 |
| A | HIS258 |
| A | ARG259 |
| A | ARG261 |
| A | MET269 |
| A | MN401 |
| A | 3PG403 |
| A | HOH508 |
| A | HOH530 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ARG101 |
| A | HOH556 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 406 |
| Chain | Residue |
| A | ALA226 |
| A | PRO227 |
| A | THR276 |
| A | SER279 |
| A | ARG280 |
| A | SER311 |
| A | LEU312 |
| A | ASP314 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 407 |
| Chain | Residue |
| A | ARG43 |
| A | GLY155 |
| A | GLY157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 17 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26136334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y7F","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y9X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26136334","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28625787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y9X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JQX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28625787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5JT0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26136334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y6N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Y6U","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
