Research workbench
Human CYP11B1 mutant in complex with metyrapone
Analyse Human CYP11B1 mutant in complex with metyrapone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E7F
- Type
- protein
- Length
- 472 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 11B1, mitochondrial
- EC
- 1.14.15.4
- UniProt
- P15538
- Ligands
- CHD, HEM, MYT
- Pockets
- 6 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 11B1, mitochondrial (EC 1.14.15.4) | protein | 472 | 57% helix, 10% strand | P15538 |
Ligands and binding sites
- CHD · Cholic acid · ligand · 2 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- MYT · Metyrapone · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 830 | 0.82 | 0.85 | 71 | HEM, MYT, CHD, GOL |
| 2 | 84 | 0.53 | 0.84 | 18 | empty |
| 3 | 113 | 0.52 | 0.81 | 19 | empty |
| 4 | 58 | 0.35 | 0.78 | 15 | empty |
| 5 | 73 | 0.32 | 0.74 | 14 | empty |
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 P15538
- Elsewhere: RCSB PDB 7E7F · PDBe 7E7F · UniProt P15538
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