Research workbench
Structure of CYP107L2 from streptomyces avermitilis with lauric acid
Analyse Structure of CYP107L2 from streptomyces avermitilis with lauric acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CWE
- Type
- protein
- Length
- 786 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 hydroxylase
- UniProt
- Q82LM3
- Ligands
- DAO, HEM, SO4
- Pockets
- 8 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cytochrome P450 hydroxylase | protein | 393 | 55% helix, 9% strand | Q82LM3 |
Ligands and binding sites
- DAO · Lauric acid · ligand · 2 copies · chains A, B
- HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 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 | 1086 | 0.88 | 0.89 | 118 | SO4, GOL |
| 2 | 935 | 0.87 | 0.88 | 80 | DAO, HEM |
| 3 | 880 | 0.86 | 0.87 | 70 | DAO, HEM |
| 4 | 240 | 0.62 | 0.81 | 35 | empty |
| 5 | 81 | 0.48 | 0.83 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1284 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 5CWE · Structure of CYP107L2 from Streptomyces avermitilis with lauric acid · 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 Q82LM3
- Elsewhere: RCSB PDB 5CWE · PDBe 5CWE · UniProt Q82LM3
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