Research workbench
Crystal structure of human gamma-aminobutyric acid receptor-associated protein-like 1 (GABARAP1), isoform CRA_A
Analyse Crystal structure of human gamma-aminobutyric acid receptor-associated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R2Q
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-aminobutyric acid receptor-associated protein-like 1
- UniProt
- Q9H0R8
- Ligands
- UNX
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Gamma-aminobutyric acid receptor-associated protein-like 1 | protein | 110 | 35% helix, 24% strand | Q9H0R8 |
Ligands and binding sites
- UNX · Unknown atom or ion · ion · 3 copies · chains A, B
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · chains 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 620 | 0.68 | 0.77 | 54 | UNX |
Interfaces
1 interface between chains.
- A–B · 342 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2R2Q · Crystal structure of human Gamma-Aminobutyric Acid Receptor-Associated Protein-like 1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H0R8 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid receptor-associated… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9H0R8
- Elsewhere: RCSB PDB 2R2Q · PDBe 2R2Q · UniProt Q9H0R8
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