Research workbench
X-ray structure of the viob N-acetyltransferase from acinetobacter baumannii in the present of tdp and acetyl-coenzymea
Analyse X-ray structure of the viob N-acetyltransferase from acinetobacter baumannii in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TXQ
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Viob
- UniProt
- A0A334FGR6
- Ligands
- TYD, ACO, NA
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Viob | protein | 209 | 16% helix, 33% strand | A0A334FGR6 |
Ligands and binding sites
- TYD · Thymidine-5'-diphosphate · ligand · chains A
- ACO · Acetyl coenzyme *A · ligand · chains A
- NA · Sodium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7TXQ · x-ray structure of the VioB N-acetyltransferase from Acinetobacter baumannii in the… · 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 A0A334FGR6
- Elsewhere: RCSB PDB 7TXQ · PDBe 7TXQ · UniProt A0A334FGR6
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.