4P3F: Human SRP68-RBD

Structure of the human SRP68-RBD. Determined by X-ray diffraction at 1.7 Å resolution. Released 16 Apr 2014.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
3,731
Mol. weight
51.78 kDa
Released
16 Apr 2014

Explore 4P3F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4P3F contains 18 α-helices and 6 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, 2 β-strands

ElementResiduesLengthSheet
β-strand5011
α-helix54-6411
α-helix67-693
α-helix72-9524
α-helix106-1072
α-helix114-13522
α-helix143-16422
β-strand17011
α-helix172-19221
α-helix196-21419
α-helix219-24325
Chain B: 9 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand5012
α-helix54-6411
α-helix67-693
α-helix72-9524
β-strand9713
β-strand10413
α-helix114-13724
α-helix141-1433
α-helix144-16522
β-strand17012
α-helix172-19221
α-helix196-21520
α-helix219-24022

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Signal recognition particle subunit SRP68A, Bprotein216Homo sapiensQ9UHB9 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4P3F_1 Signal recognition particle subunit SRP68 (chains A, B)
MGHHHHHHGSKANKEFGDSLSLEILQIIKESQQQHGLRHGDFQRYRGYCSRRQRRLRKTL
NFKMGNRHKFTGKKVTEDLLTDNRYLLLVLMDAERAWSYAMQLKQEANTEPRKRFHLLSR
LRKAVKHAEELERLCESNRVDAKTKLEAQAYTAYLSGMLRFEHQEWKAAIEAFNKCKTIY
EKLASAFTEEQAVLYNQRVEEISPNIRYCAYNIGDQ

Primary citation

SRP RNA remodeling by SRP68 explains its role in protein translocation. Grotwinkel, J.T., Wild, K., Segnitz, B. et al. Science (2014) 344:101-104. DOI 10.1126/science.1249094 · PubMed

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

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