Research workbench

Crystal structure of a death domain of human ankryn protein

Analyse Crystal structure of a death domain of human ankryn protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YVI
Type: protein
Length: 89 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ankyrin-1
UniProt: P16157

Structure

x-ray diffraction · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ankyrin-1	protein	89	76% helix, 0% strand	P16157

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Compared structures

2YVI · Crystal structure of a death domain of human ankryn protein · the same entry in another collection · chain A against A, TM-score 1.00
P16157 · AlphaFold monomer V2.0 prediction for ankyrin-1 (P16157) · a predicted model of the same protein · chain A against A, TM-score 0.93

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P16157
Elsewhere: RCSB PDB 2YVI · PDBe 2YVI · UniProt P16157

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