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The crystal structure of leishmania major N5,N10- methylenetetrahydrofolate DEHYDROGENASE/CYCLOHYDROLASE
Analyse The crystal structure of leishmania major N5,N10- methylenetetrahydrofolate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A26
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative C-1-tetrahydrofolate synthase, cytoplasmic
- EC
- 1.5.1.5, 3.5.4.9
- UniProt
- Q4Q9F9
- Ligands
- CL
- Pockets
- 6 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative C-1-tetrahydrofolate synthase, cytoplasmic (EC 1.5.1.5, 3.5.4.9) | protein | 296 | 42% helix, 17% strand | Q4Q9F9 |
| B | Putative C-1-tetrahydrofolate synthase, cytoplasmic (EC 1.5.1.5, 3.5.4.9) | protein | 290 | 42% helix, 17% strand | Q4Q9F9 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.70 | 0.89 | 29 | empty |
| 2 | 619 | 0.69 | 0.78 | 54 | empty |
| 3 | 304 | 0.59 | 0.77 | 45 | empty |
| 4 | 78 | 0.33 | 0.74 | 15 | empty |
| 5 | 62 | 0.28 | 0.73 | 9 | empty |
Interfaces
1 interface between chains.
- A–B · 1783 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
- 4A26 · The crystal structure of Leishmania major N5,N10- methylenetetrahydrofolate… · 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 Q4Q9F9
- Elsewhere: RCSB PDB 4A26 · PDBe 4A26 · UniProt Q4Q9F9
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