1QJT: PDB entry 1QJT

Name: PDB 1QJT: Solution structure of the apo EH1 domain of mouse epidermal growth factor receptor substrate 15, EPS15
Published: 2000-01-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: growth factor

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

Element	Residues	Length
α-helix	9-12	4
α-helix	18-26	9
α-helix	37-44	8
α-helix	50-60	11
α-helix	71-83	13
α-helix	91-93	3
α-helix	98-100	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor substrate substrate 15, EPS15	A	protein	99	MUS MUSCULUS	P42567 (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:

1KYF 1.22 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide
1KYU 1.8 Å, Ap-2 clathrin adaptor alpha-appendage in complex with EPS15 dpf peptide

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