Research workbench
The crystal structure of WT CYP199A4 bound to 4-chloromethylbenzoic acid
Analyse The crystal structure of WT CYP199A4 bound to 4-chloromethylbenzoic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TZX
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.414
- Source
- Rhodopseudomonas palustris
- Molecule
- Cytochrome P450
- UniProt
- Q2IU02
- Ligands
- L3C, HEM, CL
- Pockets
- 2 · best druggability 0.85
Structure
x-ray diffraction · resolution 1.414 · 1 distinct chain · 50% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 | protein | 393 | 50% helix, 13% strand | Q2IU02 |
Ligands and binding sites
- L3C · 4-(chloromethyl)benzoic acid · ligand · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CL · Chloride ion · ion · 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 | 351 | 0.85 | 0.94 | 48 | L3C, HEM |
| 2 | 135 | 0.43 | 0.76 | 24 | empty |
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 Q2IU02
- Elsewhere: RCSB PDB 7TZX · PDBe 7TZX · UniProt Q2IU02
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