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Monovalent cation binding sites in N10-formyltetrahydrofolate synthetase from moorella thermoacetica
Analyse Monovalent cation binding sites in N10-formyltetrahydrofolate synthetase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FP7
- Type
- protein
- Length
- 1,097 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formate--tetrahydrofolate ligase
- EC
- 6.3.4.3
- UniProt
- P21164
- Ligands
- K, SO4
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate--tetrahydrofolate ligase (EC 6.3.4.3) | protein | 549 | 34% helix, 17% strand | P21164 |
| B | Formate--tetrahydrofolate ligase (EC 6.3.4.3) | protein | 548 | 34% helix, 13% strand | P21164 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 736 | 0.69 | 0.76 | 69 | SO4 |
| 2 | 731 | 0.69 | 0.77 | 56 | SO4 |
| 3 | 329 | 0.69 | 0.83 | 41 | empty |
| 4 | 356 | 0.68 | 0.82 | 54 | SO4 |
| 5 | 121 | 0.49 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 26 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1FP7 · Monovalent cation binding sites in N10-formyltetrahydrofolate synthetase from moorella… · the same entry in another collection · chain A against A, TM-score 1.00
- P21164 · AlphaFold monomer V2.0 prediction for formate--tetrahydrofolate ligase (P21164) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P21164
- Elsewhere: RCSB PDB 1FP7 · PDBe 1FP7 · UniProt P21164
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