Research workbench
Crystal structure of the C-terminal domain of rat 10'FORMYLTETRAHYDROFOLATE dehydrogenase
Analyse Crystal structure of the C-terminal domain of rat 10'FORMYLTETRAHYDROFOLATE… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O2P
- Type
- protein
- Length
- 1,992 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formyltetrahydrofolate dehydrogenase
- EC
- 1.5.1.6
- UniProt
- Q5HZB2
- Ligands
- SO4
- Pockets
- 18 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) | protein | 498 | 41% helix, 23% strand | Q5HZB2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 28 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 798 | 0.88 | 0.91 | 110 | SO4 |
| 2 | 449 | 0.85 | 0.92 | 54 | SO4 |
| 3 | 422 | 0.82 | 0.90 | 41 | SO4 |
| 4 | 432 | 0.81 | 0.89 | 36 | SO4 |
| 5 | 386 | 0.81 | 0.90 | 36 | SO4 |
Interfaces
6 interfaces between chains.
- C–D · 2588 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 2555 Ų buried · 40 hydrogen bonds · protein-protein
- B–D · 1284 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 1267 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 1132 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 2O2P · Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase · 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 Q5HZB2
- Elsewhere: RCSB PDB 2O2P · PDBe 2O2P · UniProt Q5HZB2
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