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MolNFT v1 · #37206 · protein

Crystal structure of the yeast kinetochore SPC24/SPC25 globular domain

2FTX · Hypothetical 25.2 kda protein in AFG3-SEB2 intergenic region: “Crystal structure of the yeast kinetochore SPC24/SPC25 globular domain”. X-ray diffraction, 2 ligands (NA, PO4), 1 pocket (best druggability 0.28). MolNFT v1 #37206 on…

PDB
2FTX
Type
protein
Length
149 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hypothetical 25.2 kda protein in AFG3-SEB2 intergenic region; Hypothetical 24.6 kda…
UniProt
P40014, Q04477
Ligands
NA, PO4
Pockets
1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHypothetical 25.2 kda protein in AFG3-SEB2 intergenic regionprotein9042% helix, 22% strandP40014
BHypothetical 24.6 kda protein in ILV2-ADE17 intergenic regionprotein5944% helix, 20% strandQ04477

Ligands and binding sites

  • NA · Sodium ion · metal · chains A, B
  • PO4 · Phosphate ion · ion · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1520.280.7410NA

Interfaces

1 interface between chains.

  • A–B · 1228 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

  • 2FTX · Crystal structure of the yeast kinetochore Spc24/Spc25 globular domain · the same entry in another collection · chain A against A, TM-score 1.00
  • P40014 · AlphaFold monomer V2.0 prediction for kinetochore protein SPC25 (P40014) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • Q04477 · AlphaFold monomer V2.0 prediction for kinetochore protein SPC24 (Q04477) · a predicted model of the same protein · chain B against A, TM-score 0.96

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