3BQ5
Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (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 | 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 | 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 800 |
| Chain | Residue |
| A | HIS618 |
| A | CYS620 |
| A | CYS704 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 801 |
| Chain | Residue |
| B | HIS618 |
| B | CYS620 |
| B | CYS704 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE HCS A 802 |
| Chain | Residue |
| A | GLU462 |
| A | MET529 |
| A | ASP577 |
| A | HIS618 |
| A | CYS704 |
| A | GLY705 |
| A | HOH967 |
| A | ILE409 |
| A | GLY410 |
| A | SER411 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | LYS104 |
| A | PHE106 |
| A | LEU156 |
| A | HOH866 |
| A | HOH1026 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HCS B 803 |
| Chain | Residue |
| B | ILE409 |
| B | GLY410 |
| B | SER411 |
| B | GLU462 |
| B | MET529 |
| B | ASP577 |
| B | HIS618 |
| B | CYS620 |
| B | CYS704 |
| B | GLY705 |
| B | HOH896 |
| B | HOH967 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 805 |
| Chain | Residue |
| B | LYS104 |
| B | PHE106 |
| B | LEU156 |
| B | HOH835 |
| B | HOH927 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P82610 |
| Chain | Residue | Details |
| A | HIS672 | |
| B | HIS672 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15630480, ECO:0007744|PDB:1XPG, ECO:0007744|PDB:1XR2 |
| Chain | Residue | Details |
| A | ARG15 | |
| A | LYS104 | |
| A | TRP539 | |
| A | GLU583 | |
| B | ARG15 | |
| B | LYS104 | |
| B | TRP539 | |
| B | GLU583 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P82610 |
| Chain | Residue | Details |
| A | ILE409 | |
| A | GLU462 | |
| A | ASP577 | |
| B | ILE409 | |
| B | GLU462 | |
| B | ASP577 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15630480, ECO:0007744|PDB:1XR2 |
| Chain | Residue | Details |
| A | ARG493 | |
| B | ARG493 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15630480, ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ, ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ5, ECO:0007744|PDB:3BQ6 |
| Chain | Residue | Details |
| A | HIS618 | |
| A | CYS620 | |
| A | CYS704 | |
| B | HIS618 | |
| B | CYS620 | |
| B | CYS704 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15630480, ECO:0000269|PubMed:18296644, ECO:0007744|PDB:1XDJ, ECO:0007744|PDB:1XPG, ECO:0007744|PDB:3BQ6 |
| Chain | Residue | Details |
| A | GLU642 | |
| B | GLU642 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1uro |
| Chain | Residue | Details |
| A | TRP539 | |
| A | GLU464 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1uro |
| Chain | Residue | Details |
| B | TRP539 | |
| B | GLU464 |
