Research workbench
The hydrolase domain of human 10-fthfd in complex with 6- formyltetrahydropterin
Analyse The hydrolase domain of human 10-fthfd in complex with 6- formyltetrahydropterin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CFI
- Type
- protein
- Length
- 310 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
- O75891
- Ligands
- ZZZ, SO4
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) | protein | 310 | 26% helix, 27% strand | O75891 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.68 | 0.80 | 45 | ZZZ |
Compared structures
- 2CFI · The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin · the same entry in another collection · chain A against A, TM-score 1.00
- O75891 · AlphaFold monomer V2.0 prediction for cytosolic 10-formyltetrahydrofolate dehydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 O75891
- Elsewhere: RCSB PDB 2CFI · PDBe 2CFI · UniProt O75891
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