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Crystal structure of the C1QTNF5 globular domain in space group P63

Analyse Crystal structure of the C1QTNF5 globular domain in space group P63 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NN0
Type
protein
Length
416 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement C1Q tumor necrosis factor-related protein 5
UniProt
Q9BXJ0
Ligands
SO4
Pockets
3 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AComplement C1Q tumor necrosis factor-related protein 5protein1370% helix, 55% strandQ9BXJ0
BComplement C1Q tumor necrosis factor-related protein 5protein1410% helix, 53% strandQ9BXJ0
CComplement C1Q tumor necrosis factor-related protein 5protein1380% helix, 53% strandQ9BXJ0

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 3 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 18 copies · chains A, B, C
  • ACT · Acetate ion · additive · 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, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1760.580.8919ACT
2720.580.8919EDO, ACT
32190.550.7829EDO

Interfaces

2 interfaces between chains.

  • A–B · 807 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 488 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4NN0 · Crystal structure of the C1QTNF5 globular domain in space group P63 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9BXJ0 · AlphaFold monomer V2.0 prediction for complement C1Q tumor necrosis factor-related… · a predicted model of the same protein · chain A against A, TM-score 0.98

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