1QJT: PDB entry 1QJT

Solution structure of the apo EH1 domain of mouse epidermal growth factor receptor substrate 15, EPS15. Determined by solution NMR. Released 23 Jan 2000.

Method
Solution NMR
Organism
MUS MUSCULUS
Chains
1
Atoms
752
Mol. weight
10.67 kDa
Released
23 Jan 2000

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

Secondary structure: helices and β-sheets

1QJT contains 7 α-helices and 0 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: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix9-124
α-helix18-269
α-helix37-448
α-helix50-6011
α-helix71-8313
α-helix91-933
α-helix98-1003

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epidermal growth factor receptor substrate substrate 15, EPS15Aprotein99MUS MUSCULUSP42567 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1QJT_1 EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE SUBSTRATE 15, EPS15 (chains A)
LSLTQLSSGNPVYEKYYRQVEAGNTGRVLALDAAAFLKKSGLPDLILGKIWDLADTDGKG
VLSKQEFFVALRLVACAQNGLEVSLSSLSLAVPPPRFHD

Primary citation

The Eh1 Domain of Eps15 is Structurally Classified as a Member of the S100 Subclass of EF-Hand Containing Proteins. Whitehead, B., Tessari, M., Carotenuto, A. et al. Biochemistry (1999) 38:11271-11277. DOI 10.1021/BI990922I · PubMed

Other PDB entries of the same protein (UniProt P42567 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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