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Human Cytochrome P450 2A13 in complex with two molecules of 4-(methylnitrosamino)-1-(3-puridyl)-1-buta
Analyse Human Cytochrome P450 2A13 in complex with two molecules of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EJI
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Homo sapiens
- Molecule
- Cytochrome P450 2A13
- EC
- 1.14.14.1
- UniProt
- Q16696
- Ligands
- 0QA, HEM
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · resolution 2.1 · 1 distinct chain · 53% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 2A13 (EC 1.14.14.1) | protein | 464 | 53% helix, 9% strand | Q16696 |
Ligands and binding sites
- 0QA · 4-[methyl(nitroso)amino]-1-(pyridin-3-yl)butan-1-one · ligand · 2 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.87 | 0.93 | 63 | HEM, 0QA |
| 2 | 99 | 0.43 | 0.78 | 18 | 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 Q16696
- Elsewhere: RCSB PDB 4EJI · PDBe 4EJI · UniProt Q16696
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