Research workbench
Crystal structure of ATBAG3
Analyse Crystal structure of ATBAG3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HWF
- Type
- protein
- Length
- 162 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bag family molecular chaperone regulator 3
- UniProt
- Q9LYP4
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bag family molecular chaperone regulator 3 | protein | 87 | 85% helix, 0% strand | Q9LYP4 |
| B | Bag family molecular chaperone regulator 3 | protein | 75 | 72% helix, 0% strand | Q9LYP4 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 116 | 0.44 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2160 Ų buried · 16 hydrogen bonds · protein-protein
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 Q9LYP4
- Elsewhere: RCSB PDB 4HWF · PDBe 4HWF · UniProt Q9LYP4
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