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Structure of recombinant human cytochrome P450 aromatase
Analyse Structure of recombinant human cytochrome P450 aromatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KQ8
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 19A1
- EC
- 1.14.14.1
- UniProt
- P11511
- Ligands
- HEM, ASD, PO4
- Pockets
- 5 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 19A1 (EC 1.14.14.1) | protein | 452 | 55% helix, 9% strand | P11511 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- ASD · 4-androstene-3-17-dione · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 509 | 0.87 | 0.93 | 53 | HEM, ASD |
| 2 | 152 | 0.45 | 0.75 | 22 | empty |
| 3 | 77 | 0.43 | 0.80 | 14 | empty |
| 4 | 103 | 0.42 | 0.77 | 28 | empty |
| 5 | 91 | 0.38 | 0.76 | 16 | 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 P11511
- Elsewhere: RCSB PDB 4KQ8 · PDBe 4KQ8 · UniProt P11511
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