Research workbench
Crystal structure of the bacillis subtilis acetyltransferase in complex with CoA, northeast structural genomics target SR237.
Analyse Crystal structure of the bacillis subtilis 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
- 1YVK
- Type
- protein
- Length
- 608 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein BSU33890
- UniProt
- O32248
- Ligands
- COA
- Pockets
- 3 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Hypothetical protein BSU33890 | protein | 152 | 34% helix, 37% strand | O32248 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1078 | 0.85 | 0.86 | 108 | COA |
| 2 | 1183 | 0.83 | 0.84 | 113 | COA |
| 3 | 54 | 0.33 | 0.78 | 15 | empty |
Interfaces
6 interfaces between chains.
- B–C · 991 Ų buried · 19 hydrogen bonds · protein-protein
- A–D · 981 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 874 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 864 Ų buried · 22 hydrogen bonds · protein-protein
- B–D · 97 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 1YVK · Crystal Structure of the Bacillis subtilis Acetyltransferase in complex with CoA… · the same entry in another collection · chain A against A, TM-score 1.00
- O32248 · AlphaFold monomer V2.0 prediction for uncharacterized N-acetyltransferase yvbk (O32248) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O32248
- Elsewhere: RCSB PDB 1YVK · PDBe 1YVK · UniProt O32248
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