1XPG
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Methyltetrahydrofolate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003871 | molecular_function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008652 | biological_process | amino acid biosynthetic process |
| A | 0009086 | biological_process | methionine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0032259 | biological_process | methylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
| B | 0003871 | molecular_function | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008652 | biological_process | amino acid biosynthetic process |
| B | 0009086 | biological_process | methionine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032259 | biological_process | methylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071266 | biological_process | 'de novo' L-methionine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1884 |
| Chain | Residue |
| A | ARG85 |
| A | TYR388 |
| A | ARG391 |
| A | GLU635 |
| A | LYS662 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1886 |
| Chain | Residue |
| A | ARG95 |
| A | TYR490 |
| A | ARG493 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1887 |
| Chain | Residue |
| A | CYS620 |
| A | GLU642 |
| A | CYS704 |
| A | HIS618 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1885 |
| Chain | Residue |
| B | ARG85 |
| B | TYR388 |
| B | ARG391 |
| B | GLU635 |
| B | LYS662 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1888 |
| Chain | Residue |
| B | HIS618 |
| B | CYS620 |
| B | GLU642 |
| B | CYS704 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE C2F A 1882 |
| Chain | Residue |
| A | LYS18 |
| A | LYS104 |
| A | ASN109 |
| A | SER489 |
| A | ARG493 |
| A | CYS494 |
| A | TRP539 |
| A | GLU583 |
| A | HOH828 |
| A | HOH829 |
| A | HOH996 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRY B 1889 |
| Chain | Residue |
| B | PHE106 |
| B | LEU156 |
| B | CYS205 |
| B | ILE587 |
| B | HOH899 |
| B | HOH901 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE C2F B 1883 |
| Chain | Residue |
| B | ARG15 |
| B | LYS18 |
| B | LYS104 |
| B | THR466 |
| B | SER489 |
| B | SER492 |
| B | ARG493 |
| B | CYS494 |
| B | TRP539 |
| B | GLU583 |
| B | HOH759 |
| B | HOH991 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRY A 1890 |
| Chain | Residue |
| A | LYS104 |
| A | PHE106 |
| A | LEU156 |
| A | CYS205 |
| A | ILE587 |
| A | HOH791 |
| A | HOH938 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XR2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P82610","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XR2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18296644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15630480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18296644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1XDJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XPG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BQ6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
