4N3X: Rabex-5 CC domain

Crystal structure of Rabex-5 CC domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Jul 2014.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
4
Atoms
1,726
Mol. weight
24.33 kDa
Released
23 Jul 2014

Explore 4N3X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4N3X contains 5 α-helices and 0 β-strands across 4 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: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix2-1110
α-helix13-4836
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix2-5049
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix6-4641
Chain D: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix4-4845

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rab5 GDP/GTP exchange factorA, B, C, Dprotein51Homo sapiensQ9UJ41 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4N3X_1 Rab5 GDP/GTP exchange factor (chains A, B, C, D)
GSHMQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAREVQDIVEK

Primary citation

Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5. Zhang, Z., Zhang, T., Wang, S. et al. Elife (2014) 3:e02687-e02687. DOI 10.7554/eLife.02687 · PubMed

Other PDB entries of the same protein (UniProt Q9UJ41 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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