Research workbench
Crystal structure of streptomyces coelicolor A3(2) CYP158A2 from antibiotic biosynthetic pathways
Analyse Crystal structure of streptomyces coelicolor A3(2) CYP158A2 from antibiotic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SE6
- Type
- protein
- Length
- 786 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cytochrome P450
- UniProt
- Q9FCA6
- Ligands
- HEM, SPK
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 49% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cytochrome P450 | protein | 384 | 48% helix, 11% strand | Q9FCA6 |
| B | Putative cytochrome P450 | protein | 402 | 50% helix, 10% strand | Q9FCA6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SPK · Spermine (fully protonated form) · ligand · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.80 | 0.81 | 83 | HEM |
| 2 | 1063 | 0.79 | 0.81 | 87 | HEM |
| 3 | 83 | 0.38 | 0.77 | 24 | empty |
| 4 | 92 | 0.37 | 0.75 | 23 | empty |
| 5 | 85 | 0.35 | 0.75 | 23 | empty |
Compared structures
- 1SE6 · Crystal Structure of Streptomyces Coelicolor A3(2) CYP158A2 from antibiotic biosynthetic… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FCA6 · AlphaFold monomer V2.0 prediction for biflaviolin synthase CYP158A2 (Q9FCA6) · 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 Q9FCA6
- Elsewhere: RCSB PDB 1SE6 · PDBe 1SE6 · UniProt Q9FCA6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.