Research workbench
Ferredoxin-NADP+ reductase from plasmodium falciparum
Analyse Ferredoxin-NADP+ reductase from plasmodium falciparum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OK8
- Type
- protein
- Length
- 1,043 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ferredoxin--NADP reductase
- EC
- 1.18.1.2
- UniProt
- Q6LF82
- Ligands
- FAD
- Pockets
- 8 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 263 | 30% helix, 29% strand | Q6LF82 |
| B | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 262 | 27% helix, 30% strand | Q6LF82 |
| C | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 257 | 29% helix, 29% strand | Q6LF82 |
| D | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 261 | 29% helix, 29% strand | Q6LF82 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- FLC · Citrate anion · additive · 2 copies · chains A, B, D
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 | 394 | 0.69 | 0.82 | 43 | FAD |
| 2 | 372 | 0.67 | 0.80 | 46 | FAD |
| 3 | 326 | 0.64 | 0.80 | 45 | FAD |
| 4 | 250 | 0.64 | 0.82 | 39 | FAD |
| 5 | 93 | 0.39 | 0.76 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 733 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 649 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 515 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 454 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2OK8 · Ferredoxin-NADP+ reductase from Plasmodium falciparum · 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 Q6LF82
- Elsewhere: RCSB PDB 2OK8 · PDBe 2OK8 · UniProt Q6LF82
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