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The 1.92 a structure of streptomyces coelicolor A3(2) CYP154C1: a new monooxygenase that functionalizes macrolide ring systems
Analyse The 1.92 a structure of streptomyces coelicolor A3(2) CYP154C1: a new… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GWI
- Type
- protein
- Length
- 802 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 154C1
- UniProt
- Q9L142
- Ligands
- HEM, SO4
- Pockets
- 8 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 154C1 | protein | 402 | 52% helix, 11% strand | Q9L142 |
| B | Cytochrome P450 154C1 | protein | 400 | 53% helix, 12% strand | Q9L142 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 924 | 0.88 | 0.89 | 110 | SO4, HEM |
| 2 | 510 | 0.84 | 0.90 | 57 | HEM |
| 3 | 175 | 0.54 | 0.80 | 28 | empty |
| 4 | 191 | 0.53 | 0.79 | 26 | empty |
| 5 | 93 | 0.37 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 671 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 1GWI · The 1.92 A structure of Streptomyces coelicolor A3(2) CYP154C1: A new monooxygenase that… · 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 Q9L142
- Elsewhere: RCSB PDB 1GWI · PDBe 1GWI · UniProt Q9L142
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