1P4U: GGA3 gae domain

Crystal structure of GGA3 gae domain in complex with rabaptin-5 peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 29 Jul 2003.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
2
Atoms
1,373
Mol. weight
17.84 kDa
Released
29 Jul 2003

Explore 1P4U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1P4U contains 6 α-helices and 17 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: 6 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix588-5903
α-helix591-5922
β-strand59311
α-helix597-5982
β-strand599-60462
β-strand607-61372
β-strand61411
β-strand624-633102
β-strand63913
β-strand640-64784
β-strand64915
β-strand653-65642
α-helix657-6593
β-strand66413
α-helix665-6673
β-strand66816
β-strand67116
β-strand675-68392
β-strand692-70094
β-strand703-71194
α-helix717-7193
Chain B: 0 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand015
β-strand414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ADP-ribosylation factor binding protein GGA3Aprotein153Homo sapiensQ9NZ52 (AlphaFold model)
Rabaptin-5Bprotein13Q15276 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1P4U_1 ADP-ribosylation factor binding protein GGA3 (chains A)
GSPPKGPELSLASIHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVS
MLNMAPLPVKSIVLQAAAPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPLKEKV
RLRYKLTFALGEQLSTEVGEVDQFPPVEQWGNL
Sequence of entity 2 (B), FASTA
>1P4U_2 Rabaptin-5 (chains B)
DESDFGPLVGADS

Primary citation

RECOGNITION OF ACCESSORY PROTEIN MOTIFS BY THE GAMMA-ADAPTIN EAR DOMAIN OF GGA3. MILLER, G.J., MATTERA, R., BONIFACINO, J.S. et al. Nat Struct Biol (2003) 10:599-606. DOI 10.1038/nsb953 · PubMed

Other PDB entries of the same protein (UniProt Q9NZ52 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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