Research workbench
Human placental aromatase cytochrome P450 (CYP19A1) at 2.75 ångström with bound polyethylene glycol
Analyse Human placental aromatase cytochrome P450 (CYP19A1) at 2.75 ångström with bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JKV
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aromatase
- EC
- 1.14.14.14
- UniProt
- P11511
- Ligands
- HEM, ASD, PO4
- Pockets
- 6 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aromatase (EC 1.14.14.14) | protein | 452 | 53% 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 · 4 copies · chains A
- 1PE · Pentaethylene glycol · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.87 | 0.93 | 55 | HEM, ASD |
| 2 | 78 | 0.50 | 0.83 | 18 | empty |
| 3 | 178 | 0.47 | 0.75 | 24 | empty |
| 4 | 107 | 0.42 | 0.77 | 15 | empty |
| 5 | 83 | 0.40 | 0.78 | 25 | empty |
Compared structures
- 5JKV · Human placental aromatase cytochrome P450 (CYP19A1) at 2.75 ångström with bound… · the same entry in another collection · chain A against A, TM-score 1.00
- P11511 · AlphaFold monomer V2.0 prediction for aromatase (P11511) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 5JKV · PDBe 5JKV · UniProt P11511
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