3RAB: Gppnhp-bound RAB3A

Gppnhp-bound RAB3A at 2.0 a resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Apr 1999.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Rattus norvegicus
Chains
1
Atoms
1,520
Mol. weight
20.2 kDa
Ligands
GNP, MG
Released
16 Apr 1999

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

Secondary structure: helices and β-sheets

3RAB contains 8 α-helices and 8 β-strands across 1 chain. 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: 8 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand21-2881
α-helix35-4410
β-strand57-66101
β-strand69-78101
α-helix82-843
α-helix85-895
β-strand97-10371
α-helix107-1115
α-helix113-12311
β-strand129-13571
α-helix140-1423
α-helix147-15711
β-strand160-16341
β-strand16512
β-strand17012
α-helix172-18413

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (RAB3A)Aprotein169Rattus norvegicusP63012 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3RAB_1 PROTEIN (RAB3A) (chains A)
NFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWD
TAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKC
DMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEK

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31
MGMagnesium ionMg1

Primary citation

Structural basis of activation and GTP hydrolysis in Rab proteins. Dumas, J.J., Zhu, Z., Connolly, J.L. et al. Structure (1999) 7:413-423. DOI 10.1016/S0969-2126(99)80054-9 · PubMed

Other PDB entries of the same protein (UniProt P63012 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3RAB directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.