Research workbench
Crystal structure of T. maritima cobalamin-independent methionine synthase complexed with ZN2+ (monoclinic)
Analyse Crystal structure of T. maritima cobalamin-independent methionine synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BQ6
- Type
- protein
- Length
- 1,434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-methyltetrahydropteroyltriglutamate- homocysteine methyltransferase
- EC
- 2.1.1.14
- UniProt
- Q9X112
- Ligands
- ZN
- Pockets
- 13 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-methyltetrahydropteroyltriglutamate- homocysteine methyltransferase (EC 2.1.1.14) | protein | 716 | 44% helix, 14% strand | Q9X112 |
| B | 5-methyltetrahydropteroyltriglutamate- homocysteine methyltransferase (EC 2.1.1.14) | protein | 718 | 44% helix, 14% strand | Q9X112 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1040 | 0.75 | 0.78 | 74 | empty |
| 2 | 1112 | 0.74 | 0.77 | 74 | empty |
| 3 | 53 | 0.70 | 0.97 | 16 | empty |
| 4 | 50 | 0.70 | 0.98 | 17 | empty |
| 5 | 421 | 0.68 | 0.80 | 55 | empty |
Interfaces
1 interface between chains.
- A–B · 306 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3BQ6 · Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X112 · AlphaFold monomer V2.0 prediction for 5-methyltetrahydropteroyltriglutamate--homocysteine… · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9X112
- Elsewhere: RCSB PDB 3BQ6 · PDBe 3BQ6 · UniProt Q9X112
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