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Peptidyl-tRNA hydrolase from escherichia COLI

Analyse Peptidyl-tRNA hydrolase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PTH
Type: protein
Length: 193 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptidyl-tRNA hydrolase
EC: 3.1.1.29
UniProt: P0A7D1
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptidyl-tRNA hydrolase (EC 3.1.1.29)	protein	193	45% helix, 21% strand	P0A7D1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	113	0.42	0.77	26	empty

Compared structures

2PTH · Peptidyl-tRNA hydrolase from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00
P0A7D1 · AlphaFold monomer V2.0 prediction for peptidyl-tRNA hydrolase (P0A7D1) · a predicted model of the same protein · chain A against A, TM-score 0.98

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P0A7D1
Elsewhere: RCSB PDB 2PTH · PDBe 2PTH · UniProt P0A7D1

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