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Crystal structure of the peptidyl-tRNA hydrolase AF2095 from archaeglobus fulgidis. northeast structural genomics consortium target GR4

Analyse Crystal structure of the peptidyl-tRNA hydrolase AF2095 from archaeglobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ERJ
Type
protein
Length
227 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
O28185
Pockets
2 · best druggability 0.52

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APeptidyl-tRNA hydrolase (EC 3.1.1.29)protein11642% helix, 23% strandO28185
BPeptidyl-tRNA hydrolase (EC 3.1.1.29)protein11141% helix, 23% strandO28185

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.520.8220empty
2640.300.7515empty

Interfaces

1 interface between chains.

  • A–B · 952 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 3ERJ · Crystal structure of the peptidyl-tRNA hydrolase AF2095 from Archaeglobus fulgidis.… · the same entry in another collection · chain A against A, TM-score 1.00
  • O28185 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (O28185) · a predicted model of the same protein · chain A against A, TM-score 0.93

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