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Structure of scoc PT13/PT15 lir motif bound to GABARAPL1

Analyse Structure of scoc PT13/PT15 lir motif bound to GABARAPL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7AA9
Type
protein
Length
758 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gamma-aminobutyric acid receptor-associated protein-like 1; PT13/PT15 scoc lir
UniProt
Q9H0R8
Pockets
5 · best druggability 0.54

Structure

x-ray diffraction · 5 distinct chains · 31% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, E, G, KGamma-aminobutyric acid receptor-associated protein-like 1protein11733% helix, 22% strandQ9H0R8
B, H, JPT13/PT15 scoc lirprotein90% helix, 22% strand—
CGamma-aminobutyric acid receptor-associated protein-like 1protein11833% helix, 22% strandQ9H0R8
D, F, LPT13/PT15 scoc lirprotein100% helix, 20% strand—
IGamma-aminobutyric acid receptor-associated protein-like 1protein11533% helix, 21% strandQ9H0R8

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12880.540.7533empty
22410.520.7634empty
31570.430.7526empty
4910.350.7516empty
5510.270.7411empty

Interfaces

19 interfaces between chains.

  • K–L · 644 Ų buried · 10 hydrogen bonds · protein-protein
  • E–F · 641 Ų buried · 6 hydrogen bonds · protein-protein
  • A–B · 639 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 633 Ų buried · 4 hydrogen bonds · protein-protein
  • I–J · 631 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (phosphorylation).

Compared structures

  • 7AA9 · Structure of SCOC pT13/pT15 LIR motif bound to GABARAPL1 · the same entry in another collection · chain L against L, TM-score 1.00

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