MolNFT v1 · #29311 · protein
Human GCN5 acetyltransferase
1Z4R · General control of amino acid synthesis protein 5-like 2: “Human GCN5 acetyltransferase”. X-ray diffraction, 1 ligand (ACO), 1 pocket (best druggability 0.56). MolNFT v1 #29311 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1Z4R
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control of amino acid synthesis protein 5-like 2
- EC
- 2.3.1.48
- UniProt
- Q92830
- Ligands
- ACO
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General control of amino acid synthesis protein 5-like 2 (EC 2.3.1.48) | protein | 163 | 34% helix, 29% strand | Q92830 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.56 | 0.78 | 34 | ACO |
Compared structures
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 Q92830
- Elsewhere: RCSB PDB 1Z4R · PDBe 1Z4R · UniProt Q92830
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