GL1X · GenesisL1 explorer

Research workbench

Crystal structure of mutant-D97N of peptidyl-tRNA hydrolase from vibrio cholerae

Analyse Crystal structure of mutant-D97N of peptidyl-tRNA hydrolase from vibrio cholerae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5IKE
Type
protein
Length
391 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Peptidyl-tRNA hydrolase
EC
3.1.1.29
UniProt
Q9KQ21
Pockets
4 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolase (EC 3.1.1.29)protein19544% helix, 21% strandQ9KQ21
BPeptidyl-tRNA hydrolase (EC 3.1.1.29)protein19641% helix, 22% strandQ9KQ21

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.390.7617empty
2590.350.7713empty
3870.340.7417empty
4770.310.7421empty

Interfaces

1 interface between chains.

  • A–B · 1010 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (nonstandard).

Compared structures

  • 5IKE · Crystal structure of mutant-D97N of peptidyl-tRNA hydrolase from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9KQ21 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (Q9KQ21) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.