MolNFT v1 · #117500 · protein
Cytochrome P450 BM3 mutant M11
5E9Z · Bifunctional cytochrome P450/NADPH--P450 reductase: “Cytochrome P450 BM3 mutant M11”. X-ray diffraction, 2 ligands (PP9, FE2), 16 pockets (best druggability 0.87). MolNFT v1 #117500 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5E9Z
- Type
- protein
- Length
- 1,792 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bifunctional cytochrome P450/NADPH--P450 reductase
- EC
- 1.14.14.1, 1.6.2.4
- UniProt
- P14779
- Ligands
- PP9, FE2
- Pockets
- 16 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 452 | 55% helix, 12% strand | P14779 |
| B | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 451 | 54% helix, 12% strand | P14779 |
| C | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 445 | 54% helix, 12% strand | P14779 |
| D | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 444 | 54% helix, 12% strand | P14779 |
Ligands and binding sites
- PP9 · Protoporphyrin IX · ligand · 4 copies · chains A, B, C, D
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 718 | 0.87 | 0.90 | 82 | PP9, FE2 |
| 2 | 833 | 0.87 | 0.89 | 87 | PP9, FE2 |
| 3 | 930 | 0.87 | 0.88 | 106 | FE2, PP9 |
| 4 | 1066 | 0.85 | 0.86 | 106 | PP9, FE2 |
| 5 | 423 | 0.68 | 0.80 | 53 | empty |
Interfaces
3 interfaces between chains.
- A–C · 873 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 665 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 77 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 5E9Z · PDBe 5E9Z · UniProt P14779
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