Research workbench
Mthfr with mutation ASP120ALA
Analyse Mthfr with mutation ASP120ALA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PEY
- Type
- protein
- Length
- 848 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylenetetrahydrofolate reductase
- EC
- 1.5.1.20
- UniProt
- C3SIT0
- Ligands
- FAD
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylenetetrahydrofolate reductase (EC 1.5.1.20) | protein | 287 | 50% helix, 15% strand | C3SIT0 |
| B | Methylenetetrahydrofolate reductase (EC 1.5.1.20) | protein | 290 | 49% helix, 14% strand | C3SIT0 |
| C | Methylenetetrahydrofolate reductase (EC 1.5.1.20) | protein | 271 | 47% helix, 14% strand | C3SIT0 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.82 | 0.83 | 104 | FAD |
| 2 | 629 | 0.72 | 0.79 | 49 | FAD |
| 3 | 633 | 0.72 | 0.79 | 47 | FAD |
| 4 | 198 | 0.54 | 0.78 | 28 | empty |
| 5 | 88 | 0.47 | 0.81 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1375 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 725 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 214 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6PEY · MTHFR with mutation Asp120Ala · the same entry in another collection · chain A against A, TM-score 1.00
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 C3SIT0
- Elsewhere: RCSB PDB 6PEY · PDBe 6PEY · UniProt C3SIT0
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