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Crystal structure of COTB2 variant W288G
Analyse Crystal structure of COTB2 variant W288G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AO4
- Type
- protein
- Length
- 560 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclooctat-9-en-7-ol synthase
- EC
- 4.2.3.146
- UniProt
- C9K1X5
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cyclooctat-9-en-7-ol synthase (EC 4.2.3.146) | protein | 280 | 79% helix, 0% strand | C9K1X5 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 626 | 0.75 | 0.81 | 53 | MPD |
| 2 | 567 | 0.73 | 0.81 | 47 | MPD |
| 3 | 292 | 0.69 | 0.83 | 40 | empty |
| 4 | 146 | 0.59 | 0.84 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 1545 Ų buried · 30 hydrogen bonds · protein-protein
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 C9K1X5
- Elsewhere: RCSB PDB 7AO4 · PDBe 7AO4 · UniProt C9K1X5
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