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Crystal structure of the sensor domain of the transcriptional regulator hcpr from porphyromonas gingivalis

Analyse Crystal structure of the sensor domain of the transcriptional regulator hcpr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5V30
Type
protein
Length
304 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional regulator
UniProt
A0A134DM59
Ligands
SO4
Pockets
2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BTranscriptional regulatorprotein15240% helix, 28% strandA0A134DM59

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • GOL · Glycerol · additive · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12300.650.8327GOL
22010.610.8230GOL

Interfaces

1 interface between chains.

  • A–B · 2061 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 5V30 · Crystal structure of the sensor domain of the transcriptional regulator HcpR from… · the same entry in another collection · chain A against A, TM-score 1.00

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