GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the mppn domain of mouse NUP35

Analyse Crystal structure of the mppn domain of mouse NUP35 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WWH
Type
protein
Length
319 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoporin 35
UniProt
Q9D7J2
Pockets
3 · best druggability 0.37

Structure

x-ray diffraction · 3 distinct chains · 32% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANucleoporin 35protein8135% helix, 31% strandQ9D7J2
B, CNucleoporin 35protein7925% helix, 28% strandQ9D7J2
DNucleoporin 35protein8036% helix, 34% strandQ9D7J2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1760.370.7724empty
2840.370.7625empty
3620.330.7619empty

Interfaces

3 interfaces between chains.

  • C–D · 603 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 594 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 369 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1WWH · Crystal structure of the MPPN domain of mouse Nup35 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.