6WLX: PAK4 kinase domain

PAK4 kinase domain in complex with beta-catenin Ser675 substrate peptide. Determined by X-ray diffraction at 2.2 Å resolution. Released 24 Jun 2020.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
2
Atoms
2,407
Mol. weight
39.99 kDa
Released
24 Jun 2020

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

Secondary structure: helices and β-sheets

6WLX contains 22 α-helices and 13 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: 22 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix301-31111
α-helix3131
α-helix317-3193
β-strand321-32991
β-strand334-34071
β-strand346-35381
α-helix354-3563
α-helix360-3623
α-helix363-37210
β-strand37812
β-strand381-38771
β-strand390-39561
β-strand40212
α-helix403-4075
α-helix414-43320
β-strand436-43723
α-helix443-4453
β-strand446-44832
β-strand454-45632
β-strand463-46423
β-strand47214
α-helix479-4813
α-helix484-4874
β-strand49214
α-helix495-51016
α-helix520-52910
α-helix531-5355
α-helix538-5403
α-helix543-55210
α-helix561-5622
α-helix563-5664
α-helix570-5745
α-helix575-5773
α-helix578-5803
α-helix582-5843

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase PAK 4Aprotein346Homo sapiensO96013 (AlphaFold model)
Catenin beta-1Bprotein7Homo sapiensP35222 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6WLX_1 Serine/threonine-protein kinase PAK 4 (chains A)
MGSSHHHHHHSSGLVPRGSHMENLYFQGARARQENGMPEKPPGPRSPQREPQRVSHEQFR
AALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN
EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVL
QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPE
LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSL
KGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
Sequence of entity 2 (B), FASTA
>6WLX_2 Catenin beta-1 (chains B)
KKRLSVE

Primary citation

Recognition of physiological phosphorylation sites by p21-activated kinase 4. Chetty, A.K., Sexton, J.A., Ha, B.H. et al. J Struct Biol (2020) 211:107553-107553. DOI 10.1016/j.jsb.2020.107553 · PubMed

Other PDB entries of the same protein (UniProt O96013 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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