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Structure of mammalian cytochrome P450 2C5
Analyse Structure of mammalian cytochrome P450 2C5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DT6
- Type
- protein
- Length
- 449 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450 2C5
- EC
- 1.14.14.1
- UniProt
- P00179
- Ligands
- HEM, SM, SO4
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 2C5 (EC 1.14.14.1) | protein | 449 | 46% helix, 7% strand | P00179 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- SM · Samarium (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 874 | 0.86 | 0.88 | 96 | HEM |
| 2 | 101 | 0.48 | 0.81 | 14 | empty |
| 3 | 185 | 0.46 | 0.75 | 28 | empty |
| 4 | 53 | 0.27 | 0.74 | 14 | empty |
Compared structures
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 P00179
- Elsewhere: RCSB PDB 1DT6 · PDBe 1DT6 · UniProt P00179
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