MolNFT v1 · #21229 · protein
Crystal structure of the N terminal hydrolase domain of 10- formyltetrahydrofolate dehydrogenase
1S3I · 10-formyltetrahydrofolate dehydrogenase: “Crystal structure of the N terminal hydrolase domain of 10- formyltetrahydrofolate dehydrogenase”. X-ray diffraction, 1 pocket (best druggability 0.68). MolNFT v1 #21229 on GenesisL1: 3D…
- PDB
- 1S3I
- Type
- protein
- Length
- 307 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
- P28037
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 10-formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) | protein | 307 | 27% helix, 28% strand | P28037 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 5 copies · chains A
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 | 368 | 0.68 | 0.81 | 37 | BME |
Modifications
Observed in the structure: 4 covalent (additive adduct).
Compared structures
- 1S3I · Crystal structure of the N terminal hydrolase domain of 10-formyltetrahydrofolate… · the same entry in another collection · chain A against A, TM-score 1.00
- P28037 · AlphaFold monomer V2.0 prediction for cytosolic 10-formyltetrahydrofolate dehydrogenase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P28037
- Elsewhere: RCSB PDB 1S3I · PDBe 1S3I · UniProt P28037
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