5SZJ: Human Rab10

Structure of human Rab10 in complex with the bMERB domain of Mical-cL. Determined by X-ray diffraction at 2.66 Å resolution. Released 24 Aug 2016.

Method
X-ray diffraction
Resolution
2.66 Å
Organism
Homo sapiens
Chains
2
Atoms
2,638
Mol. weight
41.89 kDa
Ligands
GNP, MG
Released
24 Aug 2016

Explore 5SZJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5SZJ contains 14 α-helices and 8 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: 9 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand8-1581
α-helix22-3110
β-strand44-53101
β-strand56-65101
α-helix72-754
α-helix76-783
β-strand84-9071
α-helix94-985
α-helix100-11011
α-helix1151
β-strand116-12271
α-helix127-1293
α-helix134-14310
β-strand147-15041
β-strand15212
β-strand15712
α-helix160-17213
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix532-5343
α-helix535-57238
α-helix583-63250
α-helix635-6373
α-helix640-68142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related protein Rab-10Aprotein202Homo sapiensP61026 (AlphaFold model)
MICAL C-terminal-like proteinBprotein153Homo sapiensO94851 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5SZJ_1 Ras-related protein Rab-10 (chains A)
GHMAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKI
KLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERM
LLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKE
PNSENVDISSGGGVTGWKSKCC
Sequence of entity 2 (B), FASTA
>5SZJ_2 MICAL C-terminal-like protein (chains B)
GHMKQEELKRLYKAQAIQRQLEEVEERQRASEIQGVRLEKALRGEADSGTQDEAQLLQEW
FKLVLEKNKLMRYESELLIMAQELELEDHQSRLEQKLREKMLKEESQKDEKDLNEEQEVF
TELMQVIEQRDKLVDSLEEQRIREKAEDQHFES

Ligands and cofactors

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

Water and common crystallization additives (PEG) are not listed.

Primary citation

bMERB domains are bivalent Rab8 family effectors evolved by gene duplication. Rai, A., Oprisko, A., Campos, J. et al. Elife (2016) 5. DOI 10.7554/eLife.18675 · PubMed

Other PDB entries of the same protein (UniProt P61026 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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