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Crystal structure of the chicken cenp-T histone FOLD/CENP-W complex, crystal form I

Analyse Crystal structure of the chicken cenp-T histone FOLD/CENP-W complex, crystal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3B0C
Type
protein
Length
164 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Centromere protein T; Centromere protein W
UniProt
F1NPG5
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
TCentromere protein Tprotein9170% helix, 5% strandF1NPG5
WCentromere protein Wprotein7373% helix, 4% strand—

Ligands and binding sites

  • CIT · Citric acid · additive · 3 copies · chains T, W

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11070.510.8117empty
2580.330.7613empty

Interfaces

1 interface between chains.

  • T–W · 2374 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 3B0C · Crystal structure of the chicken CENP-T histone fold/CENP-W complex, crystal form I · the same entry in another collection · chain T against T, TM-score 1.00
  • F1NPG5 · AlphaFold monomer V2.0 prediction for centromere protein T (F1NPG5) · a predicted model of the same protein · chain T against A, TM-score 0.99

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