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Crystal structure of pcrh in complex with the chaperone binding region of popd

Analyse Crystal structure of pcrh in complex with the chaperone binding region of popd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2XCB
Type
protein
Length
273 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Regulatory protein pcrh; Pepd
UniProt
Q9I325, O50280
Ligands
NO3
Pockets
3 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 76% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARegulatory protein pcrhprotein13380% helix, 0% strandQ9I325
BRegulatory protein pcrhprotein13277% helix, 0% strandQ9I325
CPepdprotein80% helix, 0% strandO50280

Ligands and binding sites

  • NO3 · Nitrate ion · ion · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16030.700.7846empty
2810.430.8020empty
3520.290.7411empty

Interfaces

2 interfaces between chains.

  • A–B · 756 Ų buried · 8 hydrogen bonds · protein-protein
  • A–C · 534 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 2XCB · Crystal structure of PcrH in complex with the chaperone binding region of PopD · the same entry in another collection · chain A against A, TM-score 1.00

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