GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the peptide bound complex of the ankyrin repeat domains of human ANKRA2

Analyse Crystal structure of the peptide bound complex of the ankyrin repeat domains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V31
Type
protein
Length
183 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ankyrin repeat family a protein 2; Histone deacetylase 4
EC
3.5.1.98
UniProt
Q9H9E1, P56524
Ligands
ACE, NA, CL

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAnkyrin repeat family a protein 2protein16653% helix, 0% strandQ9H9E1
BHistone deacetylase 4 (EC 3.5.1.98)protein170% helix, 0% strandP56524

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A
  • CL · Chloride ion · ion · chains A

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

Interfaces

1 interface between chains.

  • A–B · 812 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

  • 3V31 · Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H9E1 · AlphaFold monomer V2.0 prediction for ankyrin repeat family a protein 2 (Q9H9E1) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • P56524 · AlphaFold monomer V2.0 prediction for histone deacetylase 4 (P56524) · a predicted model of the same protein · chain B against A, TM-score 0.21

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.