4CZ2: Ras-related protein rab-32

Complex of human VARP-ANKRD1 with Rab32-GppCp. Selenomet derivative. Determined by X-ray diffraction at 2.97 Å resolution. Released 4 Jun 2014.

Method
X-ray diffraction
Resolution
2.97 Å
Organism
HOMO SAPIENS
Chains
6
Atoms
8,249
Mol. weight
145.95 kDa
Ligands
GCP, MG
Released
4 Jun 2014

Explore 4CZ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CZ2 contains 51 α-helices and 24 β-strands across 6 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.

Chains A and C: 8 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand23-32101
α-helix38-4710
β-strand60-6781
β-strand74-8291
α-helix84-885
α-helix92-965
β-strand101-10771
α-helix112-1154
α-helix117-1259
α-helix135-1373
β-strand138-14361
α-helix155-16511
β-strand169-17241
β-strand17412
β-strand17912
α-helix181-19515
Chain B: 8 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand22-32113
α-helix38-4710
β-strand60-6783
β-strand73-82103
α-helix84-885
α-helix92-965
β-strand101-10773
α-helix112-1154
α-helix117-1259
α-helix135-1373
β-strand138-14363
α-helix155-16511
β-strand169-17243
β-strand17414
β-strand17914
α-helix181-19515
Chain D: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix466-4738
α-helix476-4849
α-helix499-5068
α-helix509-5179
α-helix532-5387
α-helix542-55110
α-helix568-5758
α-helix578-5869
α-helix608-61811
Chain E: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix466-4738
α-helix476-4849
α-helix499-5068
α-helix509-5179
α-helix532-5387
α-helix542-55110
α-helix568-5758
α-helix578-5869
α-helix608-61710
Chain F: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix466-4738
α-helix476-4849
α-helix499-5057
α-helix509-5179
α-helix532-5387
α-helix542-5509
α-helix568-5758
α-helix578-5869
α-helix608-61710

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related protein rab-32A, B, Cprotein230HOMO SAPIENSQ13637 (AlphaFold model)
Ankyrin repeat domain-containing protein 27D, E, Fprotein203HOMO SAPIENSQ96NW4 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>4CZ2_1 RAS-RELATED PROTEIN RAB-32 (chains A, B, C)
GPLGSMAGGGAGDPGLGAAAAPAPETREHLFKVLVIGELGVGKTSIIKRYVHQLFSQHYR
ATIGVDFALKVLNWDSRTLVRLQLWDIAGLERFGNMTRVYYKEAMGAFVVFDISRSSTFE
AVLKWKSDLDSKVHLPNGSPIPAVLLANKCDQNKDSSMSPSQMDQFCKEHGFAGWFETSA
KDNINIEEAARFLVEKMLVNHQSFPNEENDVDKIKLDQETLRAENKSQCC
Sequence of entity 2 (D, E, F), FASTA
>4CZ2_2 ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27 (chains D, E, F)
GPLGSMDPSVVTPFSRDDRGHTPLHVAAVCGQASLIDLLVSKGAMVNATDYHGATPLHLA
CQKGYQSVTLLLLHYKASAEVQDNNGNTPLHLACTYGHEDCVKALVYYDVESCRLDIGNE
KGDTPLHIAARWGYQGVIETLLQNGASTEIQNRLKETPLKCALNSKILSVMEAYHLSFER
RQKSSEAPVQSPQRSVDHHHHHH

Ligands and cofactors

IDNameFormulaCopies
GCPPhosphomethylphosphonic acid guanylate esterC11 H18 N5 O13 P33
MGMagnesium ionMg3

Primary citation

Varp is Recruited on to Endosomes by Direct Interaction with Retromer, Where Together They Function in Export to the Cell Surface. Hesketh, G.G., Perez-Dorado, I., Jackson, L.P. et al. Dev Cell (2014) 29:591. DOI 10.1016/J.DEVCEL.2014.04.010 · PubMed

Other PDB entries of the same protein (UniProt Q13637 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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