6JJW: KIBRA and PTPN14 complex

Crystal Structure of KIBRA and PTPN14 complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Sept 2019.

Method
X-ray diffraction
Resolution
2.4 Å
Organisms
Mus musculus, Homo sapiens
Chains
2
Atoms
960
Mol. weight
20.19 kDa
Ligands
MG
Released
25 Sept 2019

Explore 6JJW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6JJW contains 6 α-helices and 6 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: 3 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix8-92
β-strand12-1651
β-strand22-2651
β-strand31-3331
α-helix39-424
β-strand59-6462
β-strand68-7362
β-strand78-8032
α-helix84-9310
Chain U: 3 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix436-4394
α-helix441-4444
α-helix445-4517

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein KIBRAAprotein134Mus musculusQ5SXA9 (AlphaFold model)
Peptide from Tyrosine-protein phosphatase non-receptor type 14Uprotein32Homo sapiensQ15678 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6JJW_1 Protein KIBRA (chains A)
GPGSEFELPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRDRYTKPLTFADCISDELPLG
WEEAYDPQVGDYFIDHNTKTTQIEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQ
QRLELAQQEYQQLH
Sequence of entity 2 (U), FASTA
>6JJW_2 Peptide from Tyrosine-protein phosphatase non-receptor type 14 (chains U)
GPGSSHRHSAIIVPSYRPTPDYETVMRQMKRG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1

Water and common crystallization additives (GOL, FMT, CL) are not listed.

Primary citation

Decoding WW domain tandem-mediated target recognitions in tissue growth and cell polarity. Lin, Z., Yang, Z., Xie, R. et al. Elife (2019) 8. DOI 10.7554/eLife.49439 · PubMed

Other PDB entries of the same protein (UniProt Q5SXA9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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