Research workbench
Crystal structure of cytochrome P450 olet in complex with formate
Analyse Crystal structure of cytochrome P450 olet in complex with formate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M0N
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Terminal olefin-forming fatty acid decarboxylase
- UniProt
- E9NSU2
- Ligands
- HEM, SO4
- Pockets
- 3 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Terminal olefin-forming fatty acid decarboxylase | protein | 423 | 50% helix, 12% strand | E9NSU2 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 573 | 0.88 | 0.93 | 59 | HEM, FMT |
| 2 | 53 | 0.30 | 0.76 | 16 | empty |
| 3 | 60 | 0.29 | 0.75 | 14 | empty |
Compared structures
- 5M0N · Crystal structure of cytochrome P450 OleT in complex with formate · 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 E9NSU2
- Elsewhere: RCSB PDB 5M0N · PDBe 5M0N · UniProt E9NSU2
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