Research workbench
Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) from zebrafish
Analyse Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TS4
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 10-formyltetrahydrofolate dehydrogenase
- EC
- 1.5.1.6
- UniProt
- E3NZ06
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) | protein | 308 | 27% helix, 27% strand | E3NZ06 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.63 | 0.77 | 43 | empty |
| 2 | 63 | 0.28 | 0.73 | 18 | empty |
Compared structures
- 4TS4 · Crystal structure of the hydrolase domain of 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 E3NZ06
- Elsewhere: RCSB PDB 4TS4 · PDBe 4TS4 · UniProt E3NZ06
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