Research workbench
Methylenetetrahydrofolate DEHYDROGENASE/METHENYLTETRAHYDROFOLATE cyclohydrolase, putative bifunctional protein fold from francisella tularensis.
Analyse Methylenetetrahydrofolate DEHYDROGENASE/METHENYLTETRAHYDROFOLATE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3L07
- Type
- protein
- Length
- 567 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional protein fold
- EC
- 1.5.1.5, 3.5.4.9
- UniProt
- A4IYR4
- Ligands
- PO4
- Pockets
- 8 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9) | protein | 282 | 44% helix, 17% strand | A4IYR4 |
| B | Bifunctional protein fold (EC 1.5.1.5, 3.5.4.9) | protein | 285 | 44% helix, 17% strand | A4IYR4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
- IMD · Imidazole · additive · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.66 | 0.77 | 59 | IMD |
| 2 | 495 | 0.65 | 0.77 | 60 | IMD |
| 3 | 186 | 0.45 | 0.74 | 29 | EDO |
| 4 | 106 | 0.39 | 0.75 | 20 | ACT |
| 5 | 69 | 0.35 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1583 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 3L07 · Methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase, putative… · the same entry in another collection · chain A against A, TM-score 1.00
- A4IYR4 · AlphaFold monomer V2.0 prediction for bifunctional protein fold (A4IYR4) · 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 A4IYR4
- Elsewhere: RCSB PDB 3L07 · PDBe 3L07 · UniProt A4IYR4
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