4PXJ: PDB entry 4PXJ

Crystallographic structure of the LZII fragment (anti-parallel orientation) from JIP3. Determined by X-ray diffraction at 2.06 Å resolution. Released 10 Jun 2015.

Method: X-ray diffraction
Resolution: 2.06 Å
Organism: Homo sapiens
Chains: 3
Atoms: 1,588
Mol. weight: 21.22 kDa
Ligands: GAI
Released: 10 Jun 2015

Explore 4PXJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4PXJ contains 3 α-helices and 0 β-strands across 3 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.

Chains A and B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	431-484	54

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	432-484	53

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C-Jun-amino-terminal kinase-interacting protein 3	A, B, C	protein	61	Homo sapiens	Q9UPT6 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>4PXJ_1 C-Jun-amino-terminal kinase-interacting protein 3 (chains A, B, C)
GAMDPEFTKNALNVVKNDLIAKVDQLSGEQEVLRGELEAAKQAKVKLENRIKELEEELKR
V

Ligands and cofactors

ID	Name	Formula	Copies
GAI	Guanidine	C H5 N3	2

Water and common crystallization additives (SO4, EDO) are not listed.

Primary citation

Structure of a truncated form of leucine zipper II of JIP3 reveals an unexpected antiparallel coiled-coil arrangement. Llinas, P., Chenon, M., Nguyen, T.Q. et al. Acta Crystallogr F Struct Biol Commun (2016) 72:198-206. DOI 10.1107/S2053230X16001576 · PubMed

Other PDB entries of the same protein (UniProt Q9UPT6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8PR4 3.5 Å, Dynactin pointed end bound to JIP3
8PR2 3.8 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-LZI
8PR3 3.9 Å, Cytoplasmic dynein-1 heavy chain bound to JIP3-RH1
8PTK 10.0 Å, Composite structure of Dynein-Dynactin-JIP3-LIS1

Browse structure collections

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