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Toxin-antitoxin complex from klebsiella pneumoniae

Analyse Toxin-antitoxin complex from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BY2
Type
protein
Length
150 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Copg family transcriptional regulator; Ribonuclease vapc
EC
3.1.-.-
UniProt
W9BQC4, A0A0W8AM92
Pockets
1 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACopg family transcriptional regulatorprotein3043% helix, 0% strandW9BQC4
BRibonuclease vapc (EC 3.1.-.-)protein12056% helix, 12% strandA0A0W8AM92

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1990.580.8523empty

Interfaces

1 interface between chains.

  • A–B · 735 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 7BY2 · Toxin-antitoxin complex from Klebsiella pneumoniae · the same entry in another collection · chain A against A, TM-score 1.00

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