9C66: Mena EVH1 domain

Structure of the Mena EVH1 domain bound to the polyproline segment of PTP1B. Determined by X-ray diffraction at 1.4 Å resolution. Released 28 Aug 2024.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
2
Atoms
1,028
Mol. weight
14.22 kDa
Released
28 Aug 2024

Explore 9C66 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9C66 contains 6 α-helices and 8 β-strands across 2 chains. 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: 5 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix3-64
β-strand8-17101
β-strand22-2541
α-helix26-283
β-strand32-4091
α-helix41-433
β-strand45-5281
β-strand58-6361
α-helix64-652
β-strand71-7221
β-strand77-8151
β-strand86-9161
α-helix94-11118
Chain B: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix307-3093

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein enabled homologAprotein114Homo sapiensQ8N8S7 (AlphaFold model)
poly-proline segment of PTP1BBprotein10Homo sapiensP18031 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9C66_1 Protein enabled homolog (chains A)
SMSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVV
INCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNS
Sequence of entity 2 (B), FASTA
>9C66_2 poly-proline segment of PTP1B (chains B)
EHIPPPPRPP

Primary citation

Insights into the Interaction Landscape of the EVH1 Domain of Mena. LaComb, L., Ghosh, A., Bonanno, J.B. et al. Biochemistry (2024) 63:2183-2195. DOI 10.1021/acs.biochem.4c00331 · PubMed

Other PDB entries of the same protein (UniProt Q8N8S7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 9C66 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.