MolNFT v1 · #18867 · protein
Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19-residue P53 peptide
1Q2D · Histone acetyltransferase GCN5: “Crystal structure of tetrahymena GCN5 with bound coenzyme a and a 19-residue P53 peptide”. X-ray diffraction, 1 ligand (COA), 2 pockets (best druggability 0.53). MolNFT v1 #18867 on GenesisL1: 3D…
- PDB
- 1Q2D
- Type
- protein
- Length
- 167 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase GCN5; 19-mer peptide fragment from P53 tumor suppressor
- EC
- 2.3.1.-
- UniProt
- Q27198
- Ligands
- COA
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase GCN5 (EC 2.3.1.-) | protein | 161 | 34% helix, 30% strand | Q27198 |
| B | 19-mer peptide fragment from P53 tumor suppressor | protein | 6 | 0% helix, 0% strand | — |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.53 | 0.78 | 23 | COA |
| 2 | 188 | 0.53 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 497 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1Q2D · Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue p53 peptide · 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 Q27198
- Elsewhere: RCSB PDB 1Q2D · PDBe 1Q2D · UniProt Q27198
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