MolNFT v1 · #57999 · protein
Properties and crystal structure of methylenetetrahydrofolate reductase from thermus thermophilus HB8
3APY: “Properties and crystal structure of methylenetetrahydrofolate reductase from thermus thermophilus HB8”. X-ray diffraction, 2 ligands (FAD, CL), 20 pockets (best druggability 0.81). MolNFT v1 #57999 on GenesisL1: 3D structure…
- PDB
- 3APY
- Type
- protein
- Length
- 2,328 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylenetetrahydrofolate reductase
- EC
- 1.5.1.20
- UniProt
- Q5SLG6
- Ligands
- FAD, CL
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Methylenetetrahydrofolate reductase (EC 1.5.1.20) | protein | 291 | 49% helix, 15% strand | Q5SLG6 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- CL · Chloride ion · ion · 6 copies · chains A, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1021 | 0.81 | 0.82 | 80 | FAD |
| 2 | 1084 | 0.81 | 0.82 | 77 | FAD |
| 3 | 1056 | 0.80 | 0.82 | 78 | FAD |
| 4 | 1044 | 0.80 | 0.81 | 76 | FAD |
| 5 | 1152 | 0.79 | 0.80 | 81 | FAD |
Interfaces
8 interfaces between chains.
- A–B · 1266 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1239 Ų buried · 24 hydrogen bonds · protein-protein
- G–H · 1232 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 1222 Ų buried · 22 hydrogen bonds · protein-protein
- A–F · 399 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3APY · Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus… · 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 Q5SLG6
- Elsewhere: RCSB PDB 3APY · PDBe 3APY · UniProt Q5SLG6
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