Research workbench
5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase complexed with methyltetrahydrofolate to 2.2 angsrom resolution
Analyse 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2E7F
- Type
- protein
- Length
- 524 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase
- UniProt
- Q46389
- Ligands
- C2F, CA
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 5-methyltetrahydrofolate CORRINOID/IRON sulfur protein methyltransferase | protein | 262 | 51% helix, 16% strand | Q46389 |
Ligands and binding sites
- C2F · 5-methyl-5,6,7,8-tetrahydrofolic acid · ligand · 2 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.55 | 0.76 | 39 | C2F |
| 2 | 280 | 0.55 | 0.76 | 35 | C2F |
| 3 | 224 | 0.49 | 0.75 | 36 | CA |
Interfaces
1 interface between chains.
- A–B · 1468 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2E7F · 5-methyltetrahydrofolate corrinoid/iron sulfur protein methyltransferase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q46389 · AlphaFold monomer V2.0 prediction for 5-METHYLTETRAHYDROFOLATE:CORRINOID/IRON-sulfur… · a predicted model of the same protein · chain B 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 Q46389
- Elsewhere: RCSB PDB 2E7F · PDBe 2E7F · UniProt Q46389
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