Research workbench
The crystal structure of acinetobacter radioresistens CYP116B5 heme domain
Analyse The crystal structure of acinetobacter radioresistens CYP116B5 heme domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RO8
- Type
- protein
- Length
- 413 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 rhf
- UniProt
- G9BWN9
- Ligands
- HEM, HIS
- Pockets
- 4 · 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 rhf | protein | 413 | 55% helix, 9% strand | G9BWN9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 381 | 0.87 | 0.95 | 52 | HEM, HIS |
| 2 | 175 | 0.70 | 0.88 | 22 | empty |
| 3 | 110 | 0.53 | 0.83 | 26 | empty |
| 4 | 91 | 0.38 | 0.76 | 17 | empty |
Compared structures
- 6RO8 · The crystal structure of Acinetobacter radioresistens CYP116B5 heme domain · the same entry in another collection · 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 G9BWN9
- Elsewhere: RCSB PDB 6RO8 · PDBe 6RO8 · UniProt G9BWN9
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