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EVH1 domain from murine enabled in complex with acta peptide

Analyse EVH1 domain from murine enabled in complex with acta peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1EVH
Type: protein
Length: 116 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (mena EVH1 domain); Peptide acta
UniProt: Q03173
Ligands: ACE

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (mena EVH1 domain)	protein	111	19% helix, 49% strand	Q03173
B	Peptide acta	protein	5	0% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · chains A, B

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

Interfaces

1 interface between chains.

A–B · 374 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

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

Compared structures

1EVH · EVH1 domain from murine enabled in complex with acta peptide · the same entry in another collection · chain A against A, TM-score 1.00
Q03173 · AlphaFold monomer V2.0 prediction for protein enabled homolog (Q03173) · 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 Q03173
Elsewhere: RCSB PDB 1EVH · PDBe 1EVH · UniProt Q03173

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