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Crystal structure of the bar domain of human amphiphysin, isoform 1

Analyse Crystal structure of the bar domain of human amphiphysin, isoform 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SOG
Type: protein
Length: 197 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amphiphysin
UniProt: P49418
Ligands: K

Structure

x-ray diffraction · 1 distinct chain · 91% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amphiphysin	protein	197	91% helix, 0% strand	P49418

Ligands and binding sites

K · Potassium ion · metal · 2 copies · chains A
EDO · 1,2-ethanediol · additive · chains A

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

Compared structures

3SOG · Crystal structure of the BAR domain of human Amphiphysin, isoform 1 · the same entry in another collection · chain A against A, TM-score 1.00
P49418 · AlphaFold monomer V2.0 prediction for amphiphysin (P49418) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P49418
Elsewhere: RCSB PDB 3SOG · PDBe 3SOG · UniProt P49418

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