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Crystal structure of the C-terminal domain of nuclear pore complex component NUP116 from candida glabrata

Analyse Crystal structure of the C-terminal domain of nuclear pore complex component… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3NF5
Type
protein
Length
308 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nucleoporin NUP116
UniProt
Q6FU56
Pockets
3 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANucleoporin NUP116protein15615% helix, 29% strandQ6FU56
BNucleoporin NUP116protein15213% helix, 28% strandQ6FU56

Ligands and binding sites

  • GOL · Glycerol · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12670.620.8039GOL
21340.410.7423empty
31200.390.7422empty

Interfaces

1 interface between chains.

  • A–B · 709 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 3NF5 · Crystal structure of the C-terminal domain of nuclear pore complex component NUP116 from… · the same entry in another collection · chain A against A, TM-score 1.00

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