MolNFT v1 · #97474 · protein
Structure of the P4509 BM3 A82F F87V heme domain
4KF2 · Bifunctional P-450/NADPH-P450 reductase: “Structure of the P4509 BM3 A82F F87V heme domain”. X-ray diffraction, 1 ligand (HEM), 7 pockets (best druggability 0.87). MolNFT v1 #97474 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4KF2
- Type
- protein
- Length
- 899 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional P-450/NADPH-P450 reductase
- EC
- 1.14.14.1, 1.6.2.4
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 7 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional P-450/NADPH-P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 451 | 55% helix, 12% strand | P14779 |
| B | Bifunctional P-450/NADPH-P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 448 | 55% helix, 11% strand | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- IMD · Imidazole · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.87 | 0.88 | 104 | HEM, IMD |
| 2 | 1147 | 0.85 | 0.85 | 101 | HEM, IMD |
| 3 | 148 | 0.59 | 0.83 | 21 | empty |
| 4 | 282 | 0.53 | 0.75 | 31 | empty |
| 5 | 234 | 0.47 | 0.73 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 529 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4KF2 · Structure of the P4509 BM3 A82F F87V heme domain · the same entry in another collection · chain A against A, TM-score 1.00
- P14779 · AlphaFold monomer V2.0 prediction for bifunctional cytochrome P450/NADPH--P450 reductase… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 P14779
- Elsewhere: RCSB PDB 4KF2 · PDBe 4KF2 · UniProt P14779
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