Research workbench
Crystal structure of camphor-bound CYP101D2
Analyse Crystal structure of camphor-bound CYP101D2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NV6
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytochrome P450
- UniProt
- Q2G8A2
- Ligands
- HEM, CAM
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytochrome P450 | protein | 404 | 50% helix, 12% strand | Q2G8A2 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CAM · Camphor · ligand · chains A
- PEG · Di(hydroxyethyl)ether · 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 | 960 | 0.83 | 0.84 | 86 | HEM, CAM |
| 2 | 90 | 0.46 | 0.80 | 12 | empty |
| 3 | 70 | 0.32 | 0.75 | 13 | empty |
Compared structures
- 3NV6 · Crystal Structure of Camphor-Bound CYP101D2 · 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 Q2G8A2
- Elsewhere: RCSB PDB 3NV6 · PDBe 3NV6 · UniProt Q2G8A2
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