Research workbench
Crystal structure of CYP108D1 from novosphingobium aromaticivorans DSM12444
Analyse Crystal structure of CYP108D1 from novosphingobium aromaticivorans DSM12444 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TKT
- Type
- protein
- Length
- 411 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450
- UniProt
- Q2G3H6
- Ligands
- HEM
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 | protein | 411 | 54% helix, 13% strand | Q2G3H6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
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 | 842 | 0.83 | 0.85 | 93 | HEM |
| 2 | 65 | 0.33 | 0.76 | 15 | empty |
Compared structures
- 3TKT · Crystal structure of CYP108D1 from Novosphingobium aromaticivorans DSM12444 · 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 Q2G3H6
- Elsewhere: RCSB PDB 3TKT · PDBe 3TKT · UniProt Q2G3H6
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