Research workbench
Structure of the cytochrome P450 aryc from streptomyces roseosporus nrrl 15998
Analyse Structure of the cytochrome P450 aryc from streptomyces roseosporus nrrl 15998 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AYX
- Type
- protein
- Length
- 791 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 113A1
- UniProt
- D6AU61
- Ligands
- HEM, SO4
- Pockets
- 15 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 53% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 113A1 | protein | 395 | 53% helix, 13% strand | D6AU61 |
| B | Cytochrome P450 113A1 | protein | 396 | 53% helix, 13% strand | D6AU61 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 23 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.75 | 0.82 | 53 | HEM |
| 2 | 540 | 0.74 | 0.82 | 53 | HEM |
| 3 | 58 | 0.49 | 0.85 | 14 | empty |
| 4 | 104 | 0.46 | 0.80 | 13 | SO4 |
| 5 | 107 | 0.43 | 0.78 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 279 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7AYX · Structure of the cytochrome P450 AryC from Streptomyces roseosporus NRRL 15998 · 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 D6AU61
- Elsewhere: RCSB PDB 7AYX · PDBe 7AYX · UniProt D6AU61
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