9CBR
Methionine synthase from Thermus thermophilus HB8, Homocysteine, Folate, and Cobalamin Domains, Catalytic Conformation (Hcy-on)
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Methionine synthase | polymer | 877 | 95710.6 | 1 | UniProt (Q5SKM5) Pfam (PF02574) Pfam (PF00809) Pfam (PF02607) Pfam (PF02310) | Thermus thermophilus HB8 | 5-methyltetrahydrofolate--homocysteine methyltransferase |
| 2 | B (A) | 5-METHYL-5,6,7,8-TETRAHYDROFOLIC ACID | non-polymer | 459.5 | 1 | Chemie (C2F) | |||
| 3 | C, E (A) | ZINC ION | non-polymer | 65.4 | 2 | Chemie (ZN) | |||
| 4 | D (A) | COBALAMIN | non-polymer | 1330.4 | 1 | Chemie (B12) | |||
| 5 | F (A) | POTASSIUM ION | non-polymer | 39.1 | 1 | Chemie (K) | |||
| 6 | G (A) | ETHANAMINE | non-polymer | 45.1 | 1 | Chemie (NEH) | |||
| 7 | H, I (A) | water | water | 18.0 | 248 | Chemie (HOH) |
Sequence modifications
A: 1 - 877 (UniProt: Q5SKM5)
| PDB | External Database | Details |
|---|---|---|
| Ala 110 | Phe 110 | engineered mutation |
| Ala 123 | Glu 123 | engineered mutation |
| Ala 124 | Glu 124 | engineered mutation |
| Ala 268 | Arg 268 | engineered mutation |
| Ala 651 | Asp 651 | engineered mutation |
| Ala 652 | Pro 652 | engineered mutation |
| Ala 653 | Gly 653 | engineered mutation |
| Ala 759 | Asp 759 | engineered mutation |
| His 774 | Asn 774 | engineered mutation |
| Ala 826 | Arg 826 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 95710.6 | |
| Non-Polymers* | Number of molecules | 6 |
| Total formula weight | 2004.8 | |
| All* | Total formula weight | 97715.4 |
