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Crystal structure of the pH domain of human actin-binding protein anillin anln

Analyse Crystal structure of the pH domain of human actin-binding protein anillin anln in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y7B
Type
protein
Length
134 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin-binding protein anillin
UniProt
Q9NQW6
Pockets
1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 19% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AActin-binding protein anillinprotein13419% helix, 43% strandQ9NQW6

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 5 copies · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11930.510.7725empty

Compared structures

  • 2Y7B · Crystal structure of the PH domain of human Actin-binding protein anillin ANLN · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9NQW6 · AlphaFold monomer V2.0 prediction for anillin (Q9NQW6) · a predicted model of the same protein · chain A against A, TM-score 0.97

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