3LQX: SRP ribonucleoprotein core

SRP ribonucleoprotein core complexed with cobalt hexammine. Determined by X-ray diffraction at 1.93 Å resolution. Released 2 Mar 2010.

Method
X-ray diffraction
Resolution
1.93 Å
Organism
Escherichia coli
Chains
2
Atoms
1,741
Mol. weight
30.03 kDa
Ligands
NCO
Released
2 Mar 2010

Explore 3LQX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3LQX contains 6 α-helices and 0 β-strands across 1 chain. 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-75
α-helix24-3310
α-helix37-415
α-helix43-453
α-helix48-5710
α-helix62-7918

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Signal recognition particle proteinAprotein105Escherichia coliP0AGD7 (AlphaFold model)
Srp RNABRNA49
Sequence of entity 1 (A), FASTA
>3LQX_1 Signal recognition particle protein (chains A)
GFDLNDFLEQLRQMKNMGGMASLMGKLPGMGQIPDNVKSQMDDKVLVRMEAIINSMTMKE
RAKPEIIKGSRKRRIAAGSGMQVQDVNRLLKQFDDMQRMMKKMKK
Sequence of entity 2 (B), FASTA
>3LQX_2 SRP RNA (chains B)
GGCUCUGUUUACCAGGUCAGGUCCGAAAGGAAGCAGCCAAGGCAGAGCC

Ligands and cofactors

IDNameFormulaCopies
NCOCobalt hexammine(iii)Co H18 N68

Water and common crystallization additives (CL, K) are not listed.

Primary citation

Structural and Energetic Analysis of Metal Ions Essential to SRP Signal Recognition Domain Assembly. Batey, R.T., Doudna, J.A. Biochemistry (2002) 41:11703-11710. PubMed

Other PDB entries of the same protein (UniProt P0AGD7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3LQX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.