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Structure of the KNL1/NSL1 complex

Analyse Structure of the KNL1/NSL1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NF9
Type
protein
Length
441 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein CASC5; Kinetochore-associated protein NSL1 homolog
UniProt
Q8NG31, Q96IY1
Ligands
CL
Pockets
3 · best druggability 0.50

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein CASC5protein21641% helix, 28% strandQ8NG31
BProtein CASC5protein20737% helix, 29% strandQ8NG31
C, DKinetochore-associated protein NSL1 homologprotein90% helix, 11% strandQ96IY1

Ligands and binding sites

  • CL · Chloride ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12230.500.7634empty
21690.500.7723empty
3530.320.7714empty

Interfaces

3 interfaces between chains.

  • A–B · 750 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 594 Ų buried · 4 hydrogen bonds · protein-protein
  • B–D · 585 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 4NF9 · Structure of the Knl1/Nsl1 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8NG31 · AlphaFold monomer V2.0 prediction for kinetochore scaffold 1 (Q8NG31) · a predicted model of the same protein · chain B against A, TM-score 0.96
  • Q96IY1 · AlphaFold monomer V2.0 prediction for kinetochore-associated protein NSL1 homolog (Q96IY1) · a predicted model of the same protein · chain C against A, TM-score 0.53

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