3G2W: VHS Domain of human GGA1

VHS Domain of human GGA1 complexed with a DXXLL hinge peptide. Determined by X-ray diffraction at 2.4 Å resolution. Released 15 Dec 2009.

Method
X-ray diffraction
Resolution
2.4 Å
Organism
Homo sapiens
Chains
4
Atoms
2,393
Mol. weight
37.04 kDa
Released
15 Dec 2009

Explore 3G2W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3G2W contains 17 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix10-178
α-helix27-3913
α-helix43-5513
α-helix60-7617
α-helix79-857
α-helix88-9811
α-helix103-1064
α-helix109-12517
α-helix130-14213
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix10-178
α-helix27-3711
α-helix43-5513
α-helix60-7415
α-helix79-857
α-helix88-9811
α-helix109-12517
α-helix130-14011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ADP-ribosylation factor-binding protein GGA1A, Bprotein149Homo sapiensQ9UJY5 (AlphaFold model)
Internal peptide of the Hinge domain of ADP-ribosylation factor-binding protein GGA1C, Dprotein14Q9UJY5 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3G2W_1 ADP-ribosylation factor-binding protein GGA1 (chains A, B)
GSMEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSP
QEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILEL
LYSWTVGLPEEVKIAEAYQMLKKQGIVKS
Sequence of entity 2 (C, D), FASTA
>3G2W_2 Internal peptide of the Hinge domain of ADP-ribosylation factor-binding protein GGA1 (chains C, D)
SASVSLLDDELMSL

Primary citation

GGA autoinhibition revisited. Cramer, J.F., Gustafsen, C., Behrens, M.A. et al. Traffic (2010) 11:259-273. DOI 10.1111/j.1600-0854.2009.01017.x · PubMed

Other PDB entries of the same protein (UniProt Q9UJY5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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