6STG: Human Rab8a phosphorylated at Ser111

Human Rab8a phosphorylated at Ser111 in complex with GPPNP. Determined by X-ray diffraction at 2.5 Å resolution. Released 22 Apr 2020.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
2
Atoms
2,845
Mol. weight
42.67 kDa
Ligands
GNP, MG
Released
22 Apr 2020

Explore 6STG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6STG contains 15 α-helices and 16 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: 7 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand7-1481
α-helix21-3010
β-strand44-5291
β-strand55-6391
α-helix68-703
α-helix71-755
α-helix76-783
β-strand83-8971
α-helix93-10917
β-strand115-12171
α-helix133-14311
β-strand146-14941
β-strand15112
β-strand15612
α-helix158-17417
Chain B: 8 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand7-1483
α-helix21-299
α-helix431
β-strand44-5293
β-strand55-6393
α-helix68-703
α-helix71-755
β-strand83-8973
α-helix93-10917
β-strand115-12173
α-helix126-1283
α-helix133-14311
β-strand146-14943
β-strand15114
β-strand15614
α-helix158-17518

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related protein Rab-8AA, Bprotein178Homo sapiensP61006 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6STG_1 Ras-related protein Rab-8A (chains A, B)
MDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDT
AGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCD
VNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKKHHHHHH

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P32
MGMagnesium ionMg2

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

Primary citation

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2-mediated phosphorylation at Threonine72. Vieweg, S., Mulholland, K., Brauning, B. et al. Biochem J (2020) 477:1651-1668. DOI 10.1042/BCJ20190664 · PubMed

Other PDB entries of the same protein (UniProt P61006 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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