MolNFT v1 · #14190 · protein
Tetrahymena GCN5 with bound bisubstrate analog inhibitor
1M1D · TGCN5 histone acetyl transferase: “Tetrahymena GCN5 with bound bisubstrate analog inhibitor”. X-ray diffraction, 1 ligand (LYX), 3 pockets (best druggability 0.63). MolNFT v1 #14190 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1M1D
- Type
- protein
- Length
- 331 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TGCN5 histone acetyl transferase; Histone H3
- EC
- 2.3.1.-
- UniProt
- P02303
- Ligands
- LYX
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TGCN5 histone acetyl transferase (EC 2.3.1.-) | protein | 163 | 31% helix, 31% strand | — |
| B | Histone H3 | protein | 6 | 0% helix, 0% strand | P02303 |
| C | TGCN5 histone acetyl transferase (EC 2.3.1.-) | protein | 162 | 30% helix, 29% strand | — |
Ligands and binding sites
- LYX · N''-(2-coenzyme A)-propanoyl-lysine · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 362 | 0.63 | 0.78 | 41 | LYX |
| 2 | 56 | 0.40 | 0.81 | 17 | empty |
| 3 | 54 | 0.29 | 0.74 | 12 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1015 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 547 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 1M1D · Tetrahymena GCN5 with bound bisubstrate analog inhibitor · the same entry in another collection · chain C against C, 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 P02303
- Elsewhere: RCSB PDB 1M1D · PDBe 1M1D · UniProt P02303
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.