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Structural study on project id PH1539 from pyrococcus horikoshii OT3

Analyse Structural study on project id PH1539 from pyrococcus horikoshii OT3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2D3K
Type
protein
Length
236 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
O74017
Ligands
ZN
Pockets
2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPeptidyl-tRNA hydrolase (EC 3.1.1.29)protein11848% helix, 25% strandO74017

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11220.420.7621empty
2920.390.7718empty

Interfaces

1 interface between chains.

  • A–B · 1105 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 2D3K · Structural study on Project ID PH1539 from Pyrococcus horikoshii OT3 · the same entry in another collection · chain A against A, TM-score 1.00
  • O74017 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (O74017) · a predicted model of the same protein · chain A against A, TM-score 0.97

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