MolNFT v1 · #143478 · protein
Crystal structure of acetyltransferase eis from mycobacterium tuberculosis in complex with a lys-containing peptide
6B0U · N-acetyltransferase eis: “Crystal structure of acetyltransferase eis from mycobacterium tuberculosis in complex with a lys-containing…”. X-ray diffraction, 1 ligand (COA), 13 pockets (best druggability 0.87). MolNFT v1 #143478 on…
- PDB
- 6B0U
- Type
- protein
- Length
- 1,183 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase eis; Synthetic peptide atkapakka
- EC
- 2.3.1.-
- UniProt
- P9WFK7
- Ligands
- COA
- Pockets
- 13 · best druggability 0.87
Structure
x-ray diffraction · 5 distinct chains · 31% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase eis (EC 2.3.1.-) | protein | 392 | 30% helix, 31% strand | P9WFK7 |
| B | N-acetyltransferase eis (EC 2.3.1.-) | protein | 394 | 32% helix, 31% strand | P9WFK7 |
| C | N-acetyltransferase eis (EC 2.3.1.-) | protein | 390 | 31% helix, 31% strand | P9WFK7 |
| D | Synthetic peptide atkapakka | protein | 4 | 0% helix, 0% strand | — |
| E | Synthetic peptide atkapakka | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- COA · Coenzyme A · ligand · 5 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 994 | 0.87 | 0.88 | 117 | empty |
| 2 | 876 | 0.83 | 0.85 | 109 | COA |
| 3 | 865 | 0.76 | 0.80 | 68 | empty |
| 4 | 627 | 0.73 | 0.80 | 65 | empty |
| 5 | 58 | 0.55 | 0.89 | 20 | empty |
Interfaces
5 interfaces between chains.
- B–C · 2118 Ų buried · 28 hydrogen bonds · protein-protein
- A–C · 790 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 506 Ų buried · 5 hydrogen bonds · protein-protein
- B–E · 450 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 160 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6B0U · Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex… · the same entry in another collection · chain E against E, TM-score 1.00
- P9WFK7 · AlphaFold monomer V2.0 prediction for N-acetyltransferase eis (P9WFK7) · a predicted model of the same protein · chain C 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 P9WFK7
- Elsewhere: RCSB PDB 6B0U · PDBe 6B0U · UniProt P9WFK7
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