Research workbench
Crystal structure of protein lysine acetyltransferase RV0998 from mycobacterium tuberculosis
Analyse Crystal structure of protein lysine acetyltransferase RV0998 from mycobacterium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AVA
- Type
- protein
- Length
- 327 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysine acetyltransferase
- UniProt
- O05581
- Ligands
- ACO, MG
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysine acetyltransferase | protein | 327 | 34% helix, 28% strand | O05581 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
- MG · Magnesium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.49 | 0.78 | 22 | empty |
| 2 | 132 | 0.44 | 0.76 | 23 | ACO |
| 3 | 71 | 0.30 | 0.74 | 17 | empty |
Compared structures
- 4AVA · Crystal structure of protein lysine acetyltransferase Rv0998 from Mycobacterium… · the same entry in another collection · chain A against A, TM-score 1.00
- O05581 · AlphaFold monomer V2.0 prediction for acetyltransferase pat (O05581) · a predicted model of the same protein · chain A against A, TM-score 0.62
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 O05581
- Elsewhere: RCSB PDB 4AVA · PDBe 4AVA · UniProt O05581
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