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Crystal structure of quintuple arg-to-lys variant of T. celer L30E

Analyse Crystal structure of quintuple arg-to-lys variant of T. celer L30E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3N4Z
Type
protein
Length
193 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
50S ribosomal protein L30E
UniProt
P29160
Pockets
1 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A50S ribosomal protein L30Eprotein9746% helix, 20% strandP29160
B50S ribosomal protein L30Eprotein9647% helix, 20% strandP29160

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12800.590.7829empty

Interfaces

1 interface between chains.

  • A–B · 302 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3N4Z · Crystal structure of quintuple Arg-to-Lys variant of T. celer L30e · the same entry in another collection · chain A against A, TM-score 1.00
  • P29160 · AlphaFold monomer V2.0 prediction for 50S ribosomal protein L30E (P29160) · a predicted model of the same protein · chain A against A, TM-score 0.98

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