Research workbench
Crystal structure of the bromodomain of human GCN5, the general control of amino-acid synthesis protein 5-like 2
Analyse Crystal structure of the bromodomain of human GCN5, the general control of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3D7C
- Type
- protein
- Length
- 217 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control of amino acid synthesis protein 5-like 2
- UniProt
- Q92830
- Pockets
- 4 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General control of amino acid synthesis protein 5-like 2 | protein | 111 | 66% helix, 0% strand | Q92830 |
| B | General control of amino acid synthesis protein 5-like 2 | protein | 106 | 64% helix, 0% strand | Q92830 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.55 | 0.84 | 22 | empty |
| 2 | 121 | 0.55 | 0.82 | 23 | empty |
| 3 | 128 | 0.43 | 0.76 | 23 | empty |
| 4 | 103 | 0.43 | 0.78 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3D7C · Crystal structure of the bromodomain of human GCN5, the general control of amino-acid… · the same entry in another collection · chain A against A, TM-score 1.00
- Q92830 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT2A (Q92830) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 3D7C · PDBe 3D7C · UniProt Q92830
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