MolNFT v1 · #46958 · protein
Ferredoxin-NADP+ reductase from plasmodium falciparum with 2'P-AMP
2OK7 · Putative ferredoxin--NADP reductase: “Ferredoxin-NADP+ reductase from plasmodium falciparum with 2'P-AMP”. X-ray diffraction, 3 ligands (FAD, A2P, NA), 19 pockets (best druggability 0.85). MolNFT v1 #46958 on GenesisL1: 3D…
- PDB
- 2OK7
- Type
- protein
- Length
- 1,562 residues
- Chains
- 6
- 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, A2P, NA
- Pockets
- 19 · best druggability 0.85
Structure
x-ray diffraction · 6 distinct chains · 25% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 262 | 27% helix, 28% strand | Q6LF82 |
| B | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 261 | 26% helix, 29% strand | Q6LF82 |
| C | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 266 | 26% helix, 29% strand | Q6LF82 |
| D | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 262 | 25% helix, 29% strand | Q6LF82 |
| E | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 254 | 24% helix, 30% strand | Q6LF82 |
| F | Putative ferredoxin--NADP reductase (EC 1.18.1.2) | protein | 257 | 24% helix, 28% strand | Q6LF82 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 6 copies · chains A, B, C, D, E, F
- A2P · Adenosine-2'-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.85 | 0.86 | 107 | FAD, A2P |
| 2 | 785 | 0.85 | 0.88 | 100 | FAD, A2P |
| 3 | 744 | 0.85 | 0.88 | 92 | NA, FAD, A2P |
| 4 | 287 | 0.58 | 0.78 | 43 | empty |
| 5 | 63 | 0.51 | 0.86 | 18 | FAD |
Interfaces
6 interfaces between chains.
- A–B · 1135 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 961 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 951 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 668 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 442 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2OK7 · Ferredoxin-NADP+ reductase from Plasmodium falciparum with 2'P-AMP · 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 2OK7 · PDBe 2OK7 · UniProt Q6LF82
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