MolNFT v1 · #41067 · protein
The crystal structure of 5-formyl-tetrahydrofolate cycloligase from bacillus anthracis (BA4489)
2JCB · 5-formyltetrahydrofolate cyclo-ligase family protein: “The crystal structure of 5-formyl-tetrahydrofolate cycloligase from bacillus anthracis (BA4489)”. X-ray diffraction, 3 ligands (ADP, MG, PO4), 3 pockets (best druggability…
- PDB
- 2JCB
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5-formyltetrahydrofolate cyclo-ligase family protein
- EC
- 6.3.3.2
- UniProt
- Q81LX0
- Ligands
- ADP, MG, PO4
- Pockets
- 3 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5-formyltetrahydrofolate cyclo-ligase family protein (EC 6.3.3.2) | protein | 194 | 35% helix, 26% strand | Q81LX0 |
| B | 5-formyltetrahydrofolate cyclo-ligase family protein (EC 6.3.3.2) | protein | 190 | 35% helix, 23% strand | Q81LX0 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 691 | 0.78 | 0.83 | 72 | ADP, PO4, MG |
| 2 | 54 | 0.67 | 0.96 | 18 | empty |
| 3 | 271 | 0.67 | 0.83 | 39 | ADP, PO4, MG |
Interfaces
1 interface between chains.
- A–B · 524 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2JCB · The crystal structure of 5-formyl-tetrahydrofolate cycloligase from Bacillus anthracis… · 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 Q81LX0
- Elsewhere: RCSB PDB 2JCB · PDBe 2JCB · UniProt Q81LX0
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