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Structure of C. elegans htp-1 bound to htp-3 motif-1

Analyse Structure of C. elegans htp-1 bound to htp-3 motif-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4TZQ
Type
protein
Length
496 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein htp-1; Protein htp-3
UniProt
Q20305, O01820
Pockets
4 · best druggability 0.35

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein htp-1protein23331% helix, 27% strandQ20305
B, DProtein htp-3protein130% helix, 77% strandO01820
CProtein htp-1protein23730% helix, 28% strandQ20305

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11050.350.7421empty
2770.330.7414empty
3580.290.7413empty
4540.260.7420empty

Interfaces

5 interfaces between chains.

  • C–D · 1111 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1032 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 64 Ų buried · 1 hydrogen bond · protein-protein
  • A–D · 34 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 31 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4TZQ · Structure of C. elegans HTP-1 bound to HTP-3 motif-1 · the same entry in another collection · chain A against A, TM-score 1.00

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