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Crystal structure of an N-acetyltransferase, C80T mutant, from helicobacter pullorum in the presence of acetyl coenzyme a and dtdp
Analyse Crystal structure of an N-acetyltransferase, C80T mutant, from helicobacter… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7S45
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase
- Ligands
- TYD, ACO
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase | protein | 141 | 0% helix, 31% strand | — |
Ligands and binding sites
- TYD · Thymidine-5'-diphosphate · ligand · chains A
- ACO · Acetyl coenzyme *A · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- MPO · 3[N-morpholino]propane sulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7S45 · Crystal structure of an N-acetyltransferase, C80T mutant, from Helicobacter pullorum in… · 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
- Elsewhere: RCSB PDB 7S45 · PDBe 7S45
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