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Salivary protein from culex quinquefasciatus that belongs to the cysteins and tryptophan-rich (cwrc) family

Analyse Salivary protein from culex quinquefasciatus that belongs to the cysteins and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KC8
Type
protein
Length
559 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
16.4 kda salivary peptide
UniProt
Q6TS05
Pockets
3 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B16.4 kda salivary peptideprotein1400% helix, 49% strandQ6TS05
C16.4 kda salivary peptideprotein1380% helix, 50% strandQ6TS05
D16.4 kda salivary peptideprotein1410% helix, 48% strandQ6TS05

Ligands and binding sites

  • ACY · Acetic acid · additive · 3 copies · chains A, C, D

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
18330.700.76103ACY
24380.680.7969empty
32390.510.7635empty

Interfaces

6 interfaces between chains.

  • C–D · 397 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 388 Ų buried · 4 hydrogen bonds · protein-protein
  • A–C · 266 Ų buried · 0 hydrogen bonds · protein-protein
  • A–D · 173 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 165 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

  • 7KC8 · Salivary protein from Culex quinquefasciatus that belongs to the Cysteins and… · the same entry in another collection · chain A against A, TM-score 1.00

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