Research workbench
Tact complexed with acetyl-glycyl-trnagly
Analyse Tact complexed with acetyl-glycyl-trnagly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F36
- Type
- protein + RNA
- Length
- 931 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase domain-containing protein; RNA (76-mer)
- UniProt
- Q8ZL98
- Ligands
- AAC, CA
- Pockets
- 19 · best druggability 0.80
Structure
x-ray diffraction · 6 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | N-acetyltransferase domain-containing protein | protein | 159 | 33% helix, 30% strand | Q8ZL98 |
| B | N-acetyltransferase domain-containing protein | protein | 158 | 34% helix, 29% strand | Q8ZL98 |
| F, G | RNA (76-mer) | rna | 76 | — | — |
| C | N-acetyltransferase domain-containing protein | protein | 158 | 35% helix, 29% strand | Q8ZL98 |
| H | RNA (76-mer) | rna | 72 | — | — |
| E | RNA (76-mer) | rna | 73 | — | — |
Ligands and binding sites
- AAC · Acetylamino-acetic acid · ligand · chains B, E
- CA · Calcium ion · metal · 41 copies · chains A, B, F, D, C, G, H, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.80 | 0.83 | 104 | empty |
| 2 | 419 | 0.73 | 0.83 | 54 | empty |
| 3 | 410 | 0.67 | 0.79 | 53 | empty |
| 4 | 795 | 0.67 | 0.75 | 42 | CA |
| 5 | 467 | 0.63 | 0.77 | 28 | empty |
Interfaces
13 interfaces between chains.
- A–B · 1179 Ų buried · 26 hydrogen bonds · protein-protein
- D–C · 1109 Ų buried · 24 hydrogen bonds · protein-protein
- D–G · 478 Ų buried · 12 hydrogen bonds · protein-nucleic
- A–F · 471 Ų buried · 16 hydrogen bonds · protein-nucleic
- B–E · 443 Ų buried · 13 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 7F36 · TacT complexed with acetyl-glycyl-tRNAGly · 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 Q8ZL98
- Elsewhere: RCSB PDB 7F36 · PDBe 7F36 · UniProt Q8ZL98
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