Research workbench
X-ray structure of GDP-perosamine N-acetyltransferase in complex with transition state analog at 0.9 ångström resolution
Analyse X-ray structure of GDP-perosamine N-acetyltransferase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EA9
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Perosamine N-acetyltransferase
- EC
- 2.3.1.-
- UniProt
- O85353
- Ligands
- JBT, CL
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Perosamine N-acetyltransferase (EC 2.3.1.-) | protein | 207 | 16% helix, 29% strand | O85353 |
Ligands and binding sites
- JBT · GDP-N-acetylperosamine-coenzyme A · ligand · chains A
- CL · Chloride ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4EA9 · X-ray structure of GDP-perosamine N-acetyltransferase in complex with transition state… · 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 O85353
- Elsewhere: RCSB PDB 4EA9 · PDBe 4EA9 · UniProt O85353
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