Research workbench
Crystal structure of the CBP3 homolog from brucella abortus
Analyse Crystal structure of the CBP3 homolog from brucella abortus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RWT
- Type
- protein
- Length
- 181 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquinol-cytochrome C chaperone
- UniProt
- A0A0M1WEU8
- Ligands
- MG
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquinol-cytochrome C chaperone | protein | 181 | 72% helix, 0% strand | A0A0M1WEU8 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- GOL · Glycerol · additive · 2 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.49 | 0.77 | 23 | ACT |
| 2 | 57 | 0.29 | 0.74 | 13 | ACT |
Compared structures
- 6RWT · Crystal structure of the Cbp3 homolog from Brucella abortus · 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 A0A0M1WEU8
- Elsewhere: RCSB PDB 6RWT · PDBe 6RWT · UniProt A0A0M1WEU8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.