Research workbench
Structure of a putative ribosomal-protein-serine acetyltransferase from vibrio cholerae.
Analyse Structure of a putative ribosomal-protein-serine acetyltransferase from vibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FCK
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ribosomal-protein-serine acetyltransferase, putative
- UniProt
- Q9KQV9
- Ligands
- NO3
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribosomal-protein-serine acetyltransferase, putative | protein | 174 | 36% helix, 34% strand | Q9KQV9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 477 | 0.71 | 0.81 | 44 | NO3 |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2FCK · Structure of a putative ribosomal-protein-serine acetyltransferase from Vibrio cholerae. · 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 Q9KQV9
- Elsewhere: RCSB PDB 2FCK · PDBe 2FCK · UniProt Q9KQV9
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