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Crystal structure of hutp-antitermination complex

Analyse Crystal structure of hutp-antitermination complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WRQ
Type
protein + RNA
Length
300 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
5'-R(*UP*UP*UP*AP*GP*UP*U)-3'; Hut operon positive regulatory protein
UniProt
P10943
Ligands
HIS, MG
Pockets
3 · best druggability 0.38

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, D5'-R(*UP*UP*UP*AP*GP*UP*U)-3'rna7——
AHut operon positive regulatory proteinprotein14340% helix, 31% strandP10943
BHut operon positive regulatory proteinprotein14338% helix, 31% strandP10943

Ligands and binding sites

  • HIS · Histidine · ligand · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.380.7722empty
2830.340.7517empty
3580.240.7214MG, HIS

Interfaces

3 interfaces between chains.

  • A–B · 1274 Ų buried · 19 hydrogen bonds · protein-protein
  • C–A · 716 Ų buried · 20 hydrogen bonds · protein-nucleic
  • D–B · 693 Ų buried · 20 hydrogen bonds · protein-nucleic

Compared structures

  • 1WRQ · Crystal Structure of HutP-Antitermination complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P10943 · AlphaFold monomer V2.0 prediction for hut operon positive regulatory protein (P10943) · a predicted model of the same protein · chain B against A, TM-score 1.00

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