5WRW: Human apo-SRP72

Structure of human apo-SRP72. Determined by X-ray diffraction at 2.91 Å resolution. Released 21 Jun 2017.

Method: X-ray diffraction
Resolution: 2.91 Å
Organism: Homo sapiens
Chains: 6
Atoms: 6,248
Mol. weight: 111.06 kDa
Released: 21 Jun 2017

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

Secondary structure: helices and β-sheets

5WRW contains 51 α-helices and 0 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.

Chain A: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	28-40	13
α-helix	45-57	13
α-helix	61-69	9
α-helix	81-90	10
α-helix	94-102	9
α-helix	109-121	13
α-helix	125-137	13

Chain B: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	27-40	14
α-helix	45-57	13
α-helix	61-69	9
α-helix	81-90	10
α-helix	94-103	10
α-helix	109-121	13
α-helix	125-136	12

Chain C: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	27-40	14
α-helix	45-57	13
α-helix	61-70	10
α-helix	74-76	3
α-helix	81-90	10
α-helix	94-101	8
α-helix	109-121	13
α-helix	125-136	12

Chain D: 8 helices, 0 β-strands

Element	Residues	Length
α-helix	12-23	12
α-helix	27-40	14
α-helix	45-57	13
α-helix	61-70	10
α-helix	81-90	10
α-helix	94-103	10
α-helix	109-121	13
α-helix	125-137	13

Chain E: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	29-40	12
α-helix	45-57	13
α-helix	61-70	10
α-helix	73-75	3
α-helix	81-90	10
α-helix	94-102	9
α-helix	109-121	13
α-helix	125-137	13

Chain F: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	11-24	14
α-helix	27-40	14
α-helix	45-57	13
α-helix	61-69	9
α-helix	74-76	3
α-helix	81-90	10
α-helix	94-102	9
α-helix	109-121	13
α-helix	125-137	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Signal recognition particle subunit SRP72	A, B, C, D, E, F	protein	163	Homo sapiens	O76094 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>5WRW_1 Signal recognition particle subunit SRP72 (chains A, B, C, D, E, F)
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 O76094 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5M72 1.6 Å, Structure of the human SRP68-72 protein-binding domain complex
5WRV 1.7 Å, Complex structure of human SRP72/SRP68
8QVX 2.7 Å, Structure of the PBD of human SRP68/72 (cryoSPARC 3DFlex)
8QVW 3.0 Å, Cryo-EM structure of the peptide binding domain of human SRP68/72
7NFX 3.2 Å, Mammalian ribosome nascent chain complex with SRP and SRP receptor in early state A
5M73 3.4 Å, Structure of the human SRP S domain with SRP72 RNA-binding domain

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