Research workbench
Crystal structure of cytochrome P450MEL 107F1 in complex with heme and imidazole
Analyse Crystal structure of cytochrome P450MEL 107F1 in complex with heme and imidazole in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KZS
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P-450
- EC
- 1.14.-.-
- UniProt
- Q4H2B8
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 53% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P-450 (EC 1.14.-.-) | protein | 396 | 53% helix, 11% strand | Q4H2B8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.87 | 0.92 | 60 | HEM, IMD |
| 2 | 98 | 0.38 | 0.75 | 16 | empty |
Compared structures
- 6KZS · Crystal structure of cytochrome P450mel 107F1 in complex with heme and imidazole · 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 Q4H2B8
- Elsewhere: RCSB PDB 6KZS · PDBe 6KZS · UniProt Q4H2B8
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