Research workbench
Crystal structure of a mycobacterial protein
Analyse Crystal structure of a mycobacterial protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5D6N
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acyl-CoA synthase
- UniProt
- A0R618
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acyl-CoA synthase | protein | 480 | 32% helix, 25% strand | A0R618 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.55 | 0.75 | 51 | empty |
| 2 | 145 | 0.41 | 0.74 | 30 | empty |
| 3 | 64 | 0.35 | 0.78 | 17 | empty |
| 4 | 77 | 0.32 | 0.74 | 14 | empty |
| 5 | 74 | 0.32 | 0.74 | 19 | empty |
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 A0R618
- Elsewhere: RCSB PDB 5D6N · PDBe 5D6N · UniProt A0R618
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