9WS3: PAK-2p34

Crystal structure of phosphorylated PAK2 kinase domain containing K278R mutant. Determined by X-ray diffraction at 1.85 Å resolution. Released 16 Sept 2026.

Method
X-ray diffraction
Resolution
1.85 Å
Organism
Homo sapiens
Chains
1
Atoms
2,692
Mol. weight
34.99 kDa
Ligands
GAI
Released
16 Sept 2026

Explore 9WS3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WS3 contains 20 α-helices and 14 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: 20 helices, 14 β-strands

ElementResiduesLengthSheet
α-helix229-2368
β-strand24011
α-helix245-2484
β-strand249-258101
β-strand261-26881
β-strand274-28181
α-helix288-30013
β-strand30612
α-helix307-3082
β-strand309-31571
β-strand318-32471
β-strand33012
α-helix331-3355
α-helix342-36120
β-strand364-36523
α-helix371-3733
β-strand374-37632
β-strand382-38432
β-strand391-39223
β-strand40014
α-helix407-4093
α-helix412-4154
β-strand42014
α-helix424-43815
α-helix448-45811
α-helix461-4633
α-helix466-4683
α-helix471-48010
α-helix489-4902
α-helix491-4944
α-helix498-5025
α-helix503-5053
α-helix506-5094
α-helix510-52516

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PAK-2p34Aprotein309Homo sapiensQ13177 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9WS3_1 PAK-2p34 (chains A)
MASMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIRQINLQ
KQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEA
QIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTM
VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPEL
QNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSN
RLEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
GAIGuanidineC H5 N31

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

Primary citation

Kinetic and structural insights into the autoactivation of PAK2 kinase domain: A research paradigm for studying self-activating enzyme. Chen, F.Y., Hu, H.-F., Wang, J. et al. To be published.

Other PDB entries of the same protein (UniProt Q13177 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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