3BQ6
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ (Monoclinic)
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 | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 800 |
| Chain | Residue |
| A | HIS618 |
| A | CYS620 |
| A | GLU642 |
| A | CYS704 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 801 |
| Chain | Residue |
| B | HIS618 |
| B | CYS620 |
| B | GLU642 |
| B | CYS704 |
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 | 6 |
| 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 |
