MolNFT v1 · #124479 · protein
X-ray structure of a glucosamine N-acetyltransferase from clostridium acetobutylicum, mutant Y297F
5KGH · Predicted acetyltransferase: “X-ray structure of a glucosamine N-acetyltransferase from clostridium acetobutylicum, mutant Y297F”. X-ray diffraction, 2 ligands (ACO, CL), 6 pockets (best druggability 0.79). MolNFT v1 #124479 on…
- PDB
- 5KGH
- Type
- protein
- Length
- 629 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Predicted acetyltransferase
- UniProt
- Q97ML2
- Ligands
- ACO, CL
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Predicted acetyltransferase | protein | 316 | 34% helix, 32% strand | Q97ML2 |
| B | Predicted acetyltransferase | protein | 313 | 36% helix, 33% strand | Q97ML2 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 4 copies · chains A, B
- CL · Chloride ion · ion · chains B
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 490 | 0.79 | 0.86 | 47 | ACO |
| 2 | 469 | 0.78 | 0.85 | 50 | ACO |
| 3 | 479 | 0.68 | 0.79 | 67 | ACO |
| 4 | 442 | 0.68 | 0.80 | 61 | ACO |
| 5 | 121 | 0.65 | 0.88 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1425 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5KGH · X-ray structure of a glucosamine N-Acetyltransferase from Clostridium acetobutylicum… · 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 Q97ML2
- Elsewhere: RCSB PDB 5KGH · PDBe 5KGH · UniProt Q97ML2
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