MolNFT v1 · #69662 · protein
Crystal structure of bacillus megaterium BM3 heme domain mutant I401E
3KX4 · Bifunctional P-450/NADPH-P450 reductase: “Crystal structure of bacillus megaterium BM3 heme domain mutant I401E”. X-ray diffraction, 1 ligand (HEM), 6 pockets (best druggability 0.87). MolNFT v1 #69662 on GenesisL1: 3D structure…
- PDB
- 3KX4
- Type
- protein
- Length
- 907 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
- UniProt
- P14779
- Ligands
- HEM
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional P-450/NADPH-P450 reductase (EC 1.14.14.1) | protein | 453 | 55% helix, 11% strand | P14779 |
| B | Bifunctional P-450/NADPH-P450 reductase (EC 1.14.14.1) | protein | 454 | 54% helix, 11% strand | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · 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, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 784 | 0.87 | 0.89 | 88 | HEM |
| 2 | 1149 | 0.83 | 0.84 | 109 | HEM |
| 3 | 1154 | 0.75 | 0.77 | 81 | empty |
| 4 | 260 | 0.52 | 0.75 | 28 | empty |
| 5 | 193 | 0.52 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 656 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3KX4 · Crystal structure of Bacillus megaterium BM3 heme domain mutant I401E · 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 A against A, TM-score 0.99
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 3KX4 · PDBe 3KX4 · UniProt P14779
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.