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Crystal structure of assembly chaperone of ribosomal protein L4 (ACL4) in complex with ribosomal protein L4 (RPL4)

Analyse Crystal structure of assembly chaperone of ribosomal protein L4 (ACL4) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TQB
Type
protein
Length
580 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
60S ribosomal protein L4-like protein; Assembly chaperone of ribosomal protein L4 (ACL4)
UniProt
G0SFC3, G0S0I4
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A60S ribosomal protein L4-like proteinprotein24539% helix, 13% strandG0SFC3
BAssembly chaperone of ribosomal protein L4 (ACL4)protein33574% helix, 0% strandG0S0I4

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
  • PEG · Di(hydroxyethyl)ether · additive · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13440.740.8544EDO
23080.630.7927PEG
31740.580.8128empty
42310.480.7529EDO
5560.350.7915empty

Interfaces

1 interface between chains.

  • A–B · 3702 Ų buried · 55 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 5TQB · Crystal structure of assembly chaperone of ribosomal protein L4 (Acl4) in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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