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Crystal structure of ATXR5 phd domain in complex with histone H3

Analyse Crystal structure of ATXR5 phd domain in complex with histone H3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VAB
Type
protein
Length
65 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATXR5 phd domain; Histone H3 peptide
Ligands
ZN

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AATXR5 phd domainprotein546% helix, 15% strand—
FHistone H3 peptideprotein110% helix, 27% strand—

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A

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

Interfaces

1 interface between chains.

  • A–F · 607 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 5VAB · Crystal structure of ATXR5 PHD domain in complex with histone H3 · the same entry in another collection · chain A against A, TM-score 1.00

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