Research workbench
Structure of cytochrome P450 BM3 M11 mutant in complex with dtt at resolution 2.16A
Analyse Structure of cytochrome P450 BM3 M11 mutant in complex with dtt at resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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