Research workbench
Structure and function studies of cytochrome P450 158A1 from streptomyces coelicolor A3(2)
Analyse Structure and function studies of cytochrome P450 158A1 from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NZA
- Type
- protein
- Length
- 785 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 CYP158A1
- UniProt
- Q9KZF5
- Ligands
- HEM
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 CYP158A1 | protein | 397 | 45% helix, 9% strand | Q9KZF5 |
| B | Cytochrome P450 CYP158A1 | protein | 388 | 48% helix, 9% strand | Q9KZF5 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1036 | 0.82 | 0.83 | 82 | HEM |
| 2 | 852 | 0.78 | 0.81 | 72 | HEM |
| 3 | 643 | 0.68 | 0.77 | 63 | empty |
| 4 | 116 | 0.52 | 0.82 | 20 | empty |
| 5 | 59 | 0.28 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 558 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2NZA · Structure and Function Studies of Cytochrome P450 158A1 from Streptomyces coelicolor A3(2) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9KZF5 · AlphaFold monomer V2.0 prediction for biflaviolin synthase CYP158A1 (Q9KZF5) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9KZF5
- Elsewhere: RCSB PDB 2NZA · PDBe 2NZA · UniProt Q9KZF5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.