Research workbench
The crystal structure of RV2747 from mycobacterium tuberculosis in complex with CoA and nlq
Analyse The crystal structure of RV2747 from mycobacterium tuberculosis 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
- 6ADD
- Type
- protein
- Length
- 334 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amino-acid acetyltransferase
- EC
- 2.3.1.1
- UniProt
- O33289
- Ligands
- COA, NLQ
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amino-acid acetyltransferase (EC 2.3.1.1) | protein | 168 | 40% helix, 27% strand | O33289 |
| B | Amino-acid acetyltransferase (EC 2.3.1.1) | protein | 166 | 40% helix, 27% strand | O33289 |
Ligands and binding sites
- COA · Coenzyme A · ligand · 2 copies · chains A, B
- NLQ · N~2~-acetyl-L-glutamine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.80 | 0.91 | 41 | empty |
| 2 | 250 | 0.69 | 0.85 | 37 | COA, NLQ |
| 3 | 266 | 0.68 | 0.84 | 39 | COA, NLQ |
| 4 | 50 | 0.31 | 0.77 | 12 | empty |
| 5 | 57 | 0.30 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1369 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6ADD · The crystal structure of Rv2747 from Mycobacterium tuberculosis in complex with CoA and… · the same entry in another collection · chain B against B, TM-score 1.00
- O33289 · AlphaFold monomer V2.0 prediction for amino-acid acetyltransferase (O33289) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 O33289
- Elsewhere: RCSB PDB 6ADD · PDBe 6ADD · UniProt O33289
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