Research workbench
Structure of the C. glutamicum acnr crystal form II
Analyse Structure of the C. glutamicum acnr crystal form II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ACI
- Type
- protein
- Length
- 353 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional repressor acnr
- UniProt
- Q8NQ97
- Ligands
- MG, NA
- Pockets
- 7 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 80% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional repressor acnr | protein | 176 | 83% helix, 1% strand | Q8NQ97 |
| B | Hth-type transcriptional repressor acnr | protein | 177 | 77% helix, 1% strand | Q8NQ97 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · chains B
- GOL · Glycerol · additive · 2 copies · chains A
- CIT · Citric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.71 | 0.82 | 30 | empty |
| 2 | 283 | 0.68 | 0.83 | 30 | empty |
| 3 | 87 | 0.61 | 0.88 | 16 | MG, CIT |
| 4 | 83 | 0.59 | 0.88 | 17 | MG, CIT |
| 5 | 130 | 0.55 | 0.82 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1634 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4ACI · Structure of the C. glutamicum AcnR Crystal Form II · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NQ97 · AlphaFold monomer V2.0 prediction for hth-type transcriptional repressor acnr (Q8NQ97) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q8NQ97
- Elsewhere: RCSB PDB 4ACI · PDBe 4ACI · UniProt Q8NQ97
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