Research workbench
Crystal structure of gabarap fused to TEX264 lir with S272D mutation
Analyse Crystal structure of gabarap fused to TEX264 lir with S272D mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VED
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Testis-expressed protein 264,GAMMA-aminobutyric acid receptor-associated protein
- UniProt
- Q9Y6I9, O95166
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Testis-expressed protein 264,GAMMA-aminobutyric acid receptor-associated protein | protein | 129 | 33% helix, 20% strand | Q9Y6I9, O95166 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.58 | 0.76 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 309 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7VED · Crystal structure of GABARAP fused to TEX264 LIR with S272D mutation · the same entry in another collection · chain A against A, TM-score 1.00
- O95166 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid receptor-associated protein… · a predicted model of the same protein · chain A against A, TM-score 0.89
- Q9Y6I9 · AlphaFold monomer V2.0 prediction for testis-expressed protein 264 (Q9Y6I9) · a predicted model of the same protein · chain A against A, TM-score 0.35
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 Q9Y6I9
- Every structure of UniProt O95166
- Elsewhere: RCSB PDB 7VED · PDBe 7VED · UniProt Q9Y6I9 · UniProt O95166
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