4C4P: Wild-Type Rab11 Complexed to FIP2

Crystal Structure of Wild-Type Rab11 Complexed to FIP2. Determined by X-ray diffraction at 2.0 Å resolution. Released 18 Sept 2013.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
2,070
Mol. weight
32.35 kDa
Ligands
MG, GNP
Released
18 Sept 2013

Explore 4C4P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4C4P contains 10 α-helices and 7 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: 8 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand10-1781
α-helix24-3310
α-helix42-443
β-strand46-55101
β-strand58-67101
α-helix77-815
β-strand84-9291
α-helix96-1005
α-helix102-11211
β-strand118-12471
α-helix129-1313
α-helix136-14510
β-strand149-15241
α-helix161-17010
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix453-49139
α-helix493-4964
β-strand497-49821

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related protein rab-11AAprotein173HOMO SAPIENSP62491 (AlphaFold model)
RAB11 family-interacting protein 2Bprotein107HOMO SAPIENSQ7L804 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>4C4P_1 RAS-RELATED PROTEIN RAB-11A (chains A)
MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTI
KAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIM
LVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVEAAFQTILTEIY
Sequence of entity 2 (B), FASTA
>4C4P_2 RAB11 FAMILY-INTERACTING PROTEIN 2 (chains B)
GAMAAKFRASNIMPSSSFHMSPTSNEDLRKIPDSNPFDATAGYRSLTYEEVLQELVKHKE
LLRRKDTHIRELEDYIDNLLVRVMEETPSILRVPYEPSRKAGKFSNS

Ligands and cofactors

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

Primary citation

Structural and Functional Analysis of Fip2 Binding to the Endosome-Localised Rab25 Gtpase. Lall, P., Horgan, C.P., Oda, S. et al. Biochim Biophys Acta (2013) 1834:2679. DOI 10.1016/J.BBAPAP.2013.09.005 · PubMed

Other PDB entries of the same protein (UniProt P62491 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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