MolNFT v1 · #151461 · protein
Structure of BECLIN1 lir motif bound to GABARAPL1
6HOI · Gamma-aminobutyric acid receptor-associated protein-like 1: “Structure of BECLIN1 lir motif bound to GABARAPL1”. X-ray diffraction. MolNFT v1 #151461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HOI
- Type
- protein
- Length
- 251 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-aminobutyric acid receptor-associated protein-like 1; Beclin-1
- UniProt
- Q9H0R8, Q14457
Structure
x-ray diffraction · 4 distinct chains · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-aminobutyric acid receptor-associated protein-like 1 | protein | 118 | 31% helix, 22% strand | Q9H0R8 |
| B | Gamma-aminobutyric acid receptor-associated protein-like 1 | protein | 117 | 32% helix, 22% strand | Q9H0R8 |
| F | Beclin-1 | protein | 7 | 0% helix, 29% strand | Q14457 |
| G | Beclin-1 | protein | 9 | 0% helix, 22% strand | Q14457 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- A–G · 549 Ų buried · 5 hydrogen bonds · protein-protein
- B–F · 523 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 474 Ų buried · 12 hydrogen bonds · protein-protein
- B–G · 74 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6HOI · Structure of Beclin1 LIR motif bound to GABARAPL1 · the same entry in another collection · chain G against G, 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 0.96
- Q14457 · AlphaFold monomer V2.0 prediction for beclin-1 (Q14457) · a predicted model of the same protein · chain F against A, TM-score 0.65
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
- Every structure of UniProt Q14457
- Elsewhere: RCSB PDB 6HOI · PDBe 6HOI · UniProt Q9H0R8 · UniProt Q14457
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