Research workbench
Crystal structure of brucella canis acyl-CoA synthetase
Analyse Crystal structure of brucella canis acyl-CoA synthetase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U2A
- Type
- protein
- Length
- 542 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AMP-dependent synthetase and ligase
- UniProt
- A9MB96
- Ligands
- CL
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AMP-dependent synthetase and ligase | protein | 542 | 31% helix, 26% strand | A9MB96 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 438 | 0.64 | 0.78 | 64 | empty |
| 2 | 154 | 0.48 | 0.77 | 23 | empty |
| 3 | 127 | 0.43 | 0.77 | 23 | empty |
| 4 | 141 | 0.43 | 0.75 | 23 | empty |
| 5 | 112 | 0.39 | 0.75 | 29 | empty |
Compared structures
- 5U2A · Crystal structure of Brucella canis Acyl-CoA Synthetase · 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 A9MB96
- Elsewhere: RCSB PDB 5U2A · PDBe 5U2A · UniProt A9MB96
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