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MolNFT v1 · #40025 · protein

Structure of the histone H3-ASF1 chaperone interaction

2IDC · Anti-silencing protein 1 and histone H3 chimera: “Structure of the histone H3-ASF1 chaperone interaction”. X-ray diffraction. MolNFT v1 #40025 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
2IDC
Type
protein
Length
167 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Anti-silencing protein 1 and histone H3 chimera
UniProt
P32447, P61830

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnti-silencing protein 1 and histone H3 chimeraprotein16713% helix, 46% strandP32447, P61830

Compared structures

  • 2IDC · Structure of the Histone H3-Asf1 Chaperone Interaction · the same entry in another collection · chain A against A, TM-score 1.00
  • P32447 · AlphaFold monomer V2.0 prediction for histone chaperone ASF1 (P32447) · a predicted model of the same protein · chain A against A, TM-score 0.93
  • P61830 · AlphaFold monomer V2.0 prediction for histone H3 (P61830) · a predicted model of the same protein · chain A against A, TM-score 0.22

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