Research workbench
Human CYP11B2 and human adrenodoxin in complex with fadrozole
Analyse Human CYP11B2 and human adrenodoxin in complex with fadrozole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M8I
- Type
- protein
- Length
- 1,673 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adrenodoxin, cytochrome P450 11B2, mitochondrial fusion enzyme
- EC
- 1.14.15.5, 1.14.15.4
- UniProt
- P10109, P19099
- Ligands
- FES, HEM, 0T3
- Pockets
- 17 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 52% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adrenodoxin, cytochrome P450 11B2, mitochondrial fusion enzyme (EC 1.14.15.5, 1.14.15.4) | protein | 572 | 51% helix, 12% strand | P10109, P19099 |
| B | Adrenodoxin, cytochrome P450 11B2, mitochondrial fusion enzyme (EC 1.14.15.5, 1.14.15.4) | protein | 572 | 51% helix, 12% strand | P10109, P19099 |
| C | Adrenodoxin, cytochrome P450 11B2, mitochondrial fusion enzyme (EC 1.14.15.5, 1.14.15.4) | protein | 529 | 53% helix, 8% strand | P10109, P19099 |
Ligands and binding sites
- FES · Fe2/s2 (inorganic) cluster · ligand · 3 copies · chains A, B, C
- HEM · Protoporphyrin IX containing Fe · ligand · 3 copies · chains A, B, C
- 0T3 · 4-[(5R)-5,6,7,8-tetrahydroimidazo[1,5-a]pyridin-5-yl]benzonitrile · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 920 | 0.87 | 0.88 | 93 | HEM, 0T3 |
| 2 | 952 | 0.87 | 0.88 | 92 | HEM, 0T3 |
| 3 | 986 | 0.86 | 0.87 | 93 | HEM, 0T3 |
| 4 | 558 | 0.66 | 0.77 | 48 | empty |
| 5 | 568 | 0.66 | 0.76 | 44 | empty |
Interfaces
3 interfaces between chains.
- B–C · 750 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 739 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 735 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7M8I · Human CYP11B2 and human adrenodoxin in complex with fadrozole · the same entry in another collection · chain A against A, TM-score 1.00
- P19099 · AlphaFold monomer V2.0 prediction for cytochrome P450 11B2, mitochondrial (P19099) · a predicted model of the same protein · chain C against A, TM-score 0.88
- P10109 · AlphaFold monomer V2.0 prediction for adrenodoxin, mitochondrial (P10109) · a predicted model of the same protein · chain A against A, TM-score 0.20
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 P10109
- Every structure of UniProt P19099
- Elsewhere: RCSB PDB 7M8I · PDBe 7M8I · UniProt P10109 · UniProt P19099
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