1EGX: Vasodilator-stimulated phosphoprotein

Solution structure of the ena-vasp homology 1 (EVH1) domain of human vasodilator-stimulated phosphoprotein (VASP). Determined by solution NMR. Released 20 Sept 2000.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
895
Mol. weight
12.75 kDa
Released
20 Sept 2000

Explore 1EGX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1EGX contains 1 α-helix and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 10 β-strands

ElementResiduesLengthSheet
β-strand5-1061
β-strand11-1222
β-strand1413
β-strand15-1622
β-strand2513
β-strand34-4181
β-strand46-5381
β-strand60-6671
β-strand79-8352
β-strand88-9362
α-helix96-11419

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vasodilator-stimulated phosphoproteinAprotein115Homo sapiensP50552 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1EGX_1 VASODILATOR-STIMULATED PHOSPHOPROTEIN (chains A)
MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQV
VINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEG

Primary citation

Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity. Ball, L.J., Kuhne, R., Hoffmann, B. et al. EMBO J (2000) 19:4903-4914. DOI 10.1093/emboj/19.18.4903 · PubMed

Other PDB entries of the same protein (UniProt P50552 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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