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Crystal structure of the C-terminal domain of DNA topoisomerase IV

Analyse Crystal structure of the C-terminal domain of DNA topoisomerase IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WP5
Type
protein
Length
323 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Topoisomerase IV
EC
5.99.1.-
Pockets
1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATopoisomerase IV (EC 5.99.1.-)protein32313% helix, 40% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18430.720.7763empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 1WP5 · Crystal structure of the C-terminal domain of DNA topoisomerase IV · the same entry in another collection · chain A against A, TM-score 1.00

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