MolNFT v1 · #22570 · protein
Evidence for multiple substrate recognition and molecular mechanism of C-C reaction by cytochrome P450 CYP158A2 from streptomyces coelicolor A3(2)
1T93 · Putative cytochrome P450: “Evidence for multiple substrate recognition and molecular mechanism of C-C reaction by cytochrome P450…”. X-ray diffraction, 2 ligands (FLV, HEM), 5 pockets (best druggability 0.86). MolNFT v1 #22570 on…
- PDB
- 1T93
- Type
- protein
- Length
- 403 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cytochrome P450
- UniProt
- Q9FCA6
- Ligands
- FLV, HEM
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cytochrome P450 | protein | 403 | 45% helix, 10% strand | Q9FCA6 |
Ligands and binding sites
- FLV · Flaviolin · ligand · 2 copies · chains A
- HEM · Protoporphyrin IX containing Fe · ligand · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 693 | 0.86 | 0.90 | 62 | HEM, FLV |
| 2 | 128 | 0.41 | 0.75 | 28 | empty |
| 3 | 59 | 0.39 | 0.80 | 11 | empty |
| 4 | 66 | 0.37 | 0.78 | 15 | empty |
| 5 | 72 | 0.33 | 0.75 | 16 | empty |
Compared structures
- 1T93 · Evidence for Multiple Substrate Recognition and Molecular Mechanism of C-C reaction by… · 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 0.94
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 1T93 · PDBe 1T93 · UniProt Q9FCA6
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