5WRV: Complex structure of human SRP72/SRP68

Complex structure of human SRP72/SRP68. Determined by X-ray diffraction at 1.7 Å resolution. Released 21 Jun 2017.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
1,709
Mol. weight
30.9 kDa
Released
21 Jun 2017

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

Secondary structure: helices and β-sheets

5WRV contains 12 α-helices and 0 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: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix593-5975
α-helix600-6023
α-helix604-6074
Chain B: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix11-2313
α-helix27-4014
α-helix45-5713
α-helix61-699
α-helix81-9010
α-helix94-1029
α-helix109-12113
α-helix125-13814
α-helix144-15916

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Signal recognition particle subunit SRP68Aprotein106Homo sapiensQ9UHB9 (AlphaFold model)
Signal recognition particle subunit SRP72Bprotein163Homo sapiensO76094 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5WRV_1 Signal recognition particle subunit SRP68 (chains A)
DLPDVQELITQVRSEKCSLQAAAILDANDAHQTETSSSQVKDNKPLVERFETFCLDPSLV
TKQANLVHFPPGFQPIPCKPLFFDLALNHVAFPPLEDKLAAATKSG
Sequence of entity 2 (B), FASTA
>5WRV_2 Signal recognition particle subunit SRP72 (chains B)
MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGS
FKEALNVINTHTKVLANNSLSFEKAYCEYRLNRIENALKTIESANQQTDKLKELYGQVLY
RLERYDECLAVYRDLVRNSQDDYDEERKTNLSAVVAAQSNWEK

Primary citation

Human apo-SRP72 and SRP68/72 complex structures reveal the molecular basis of protein translocation. Gao, Y., Zhang, Q., Lang, Y. et al. J Mol Cell Biol (2017) 9:220-230. DOI 10.1093/jmcb/mjx010 · PubMed

Other PDB entries of the same protein (UniProt Q9UHB9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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