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Vhs domain of human GGA1 complexed with a dxxll hinge peptide

Analyse Vhs domain of human GGA1 complexed with a dxxll hinge peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3G2W
Type
protein
Length
294 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ADP-ribosylation factor-binding protein GGA1; Internal peptide of the hinge domain of…
UniProt
Q9UJY5
Pockets
2 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 67% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AADP-ribosylation factor-binding protein GGA1protein13974% helix, 0% strandQ9UJY5
BADP-ribosylation factor-binding protein GGA1protein13867% helix, 0% strandQ9UJY5
CInternal peptide of the hinge domain of ADP-ribosylation factor-binding protein GGA1protein90% helix, 0% strandQ9UJY5
DInternal peptide of the hinge domain of ADP-ribosylation factor-binding protein GGA1protein80% helix, 0% strandQ9UJY5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14430.710.8159empty
21090.480.8121empty

Interfaces

3 interfaces between chains.

  • A–B · 692 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 566 Ų buried · 12 hydrogen bonds · protein-protein
  • B–D · 504 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 3G2W · VHS Domain of human GGA1 complexed with a DXXLL hinge peptide · the same entry in another collection · chain D against D, TM-score 1.00
  • Q9UJY5 · AlphaFold monomer V2.0 prediction for ADP-ribosylation factor-binding protein GGA1… · a predicted model of the same protein · chain A against A, TM-score 0.99

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