MolNFT v1 · #152210 · protein
Structure of cytochrome P450 BM3 M11 mutant in complex with dtt at resolution 2.16A
6IAO · Bifunctional cytochrome P450/NADPH--P450 reductase: “Structure of cytochrome P450 BM3 M11 mutant in complex with dtt at resolution 2.16A”. X-ray diffraction, 2 ligands (HEM, CL), 11 pockets (best druggability 0.87). MolNFT v1…
- PDB
- 6IAO
- Type
- protein
- Length
- 1,807 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
- HEM, CL
- Pockets
- 11 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 53% 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 | 455 | 54% helix, 11% strand | P14779 |
| B | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 452 | 55% helix, 12% strand | P14779 |
| C | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 450 | 52% helix, 12% strand | P14779 |
| D | Bifunctional cytochrome P450/NADPH--P450 reductase (EC 1.14.14.1, 1.6.2.4) | protein | 450 | 53% helix, 12% strand | P14779 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 20 copies · chains A, B, C, D
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · 5 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, B, C
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 984 | 0.87 | 0.88 | 115 | HEM, DTT, CL |
| 2 | 1133 | 0.86 | 0.87 | 103 | HEM, DTT |
| 3 | 897 | 0.86 | 0.87 | 108 | HEM, DTT, CL |
| 4 | 1141 | 0.85 | 0.85 | 128 | HEM, DTT, CL |
| 5 | 183 | 0.59 | 0.82 | 33 | CL |
Interfaces
2 interfaces between chains.
- A–B · 748 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 375 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 6IAO · Structure of Cytochrome P450 BM3 M11 mutant in complex with DTT at resolution 2.16A · the same entry in another collection · chain D against D, 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 0.98
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 6IAO · PDBe 6IAO · UniProt P14779
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