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Crystal structure of the enth domain of rat epsin 1

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

PDB: 1EDU
Type: protein
Length: 149 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Eh domain binding protein epsin
UniProt: O88339

Structure

x-ray diffraction · 1 distinct chain · 72% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Eh domain binding protein epsin	protein	149	72% helix, 1% strand	O88339

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 4 copies · chains A

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

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1EDU · Crystal structure of the enth domain of rat epsin 1 · the same entry in another collection · chain A against A, TM-score 1.00
O88339 · AlphaFold monomer V2.0 prediction for epsin-1 (O88339) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 O88339
Elsewhere: RCSB PDB 1EDU · PDBe 1EDU · UniProt O88339

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