9WS6: PAK-2p34

Crystal structure of AMP-PNP-bound PAK2 kinase domain containing D368N mutant. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Sept 2026.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
4
Atoms
9,673
Mol. weight
146.15 kDa
Ligands
MG, ANP
Released
16 Sept 2026

Explore 9WS6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WS6 contains 88 α-helices and 44 β-strands across 4 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: 25 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix225-2284
α-helix229-23911
α-helix2411
α-helix245-2484
β-strand249-25791
β-strand261-26881
β-strand274-28181
α-helix282-2843
α-helix289-30012
β-strand30612
α-helix307-3082
β-strand309-31461
β-strand318-32471
β-strand33012
α-helix331-3377
α-helix342-36120
β-strand364-36523
α-helix371-3733
β-strand374-37632
β-strand382-38432
α-helix387-3893
β-strand391-39223
α-helix397-4004
β-strand404-40524
α-helix407-4093
α-helix412-4154
α-helix423-43816
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-helix510-52112
Chain B: 20 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix233-2375
α-helix245-2484
β-strand249-25795
β-strand262-26875
β-strand273-28195
α-helix282-2843
α-helix288-30013
β-strand30616
α-helix307-3082
β-strand309-31575
β-strand318-32475
β-strand33016
α-helix331-3377
α-helix342-36120
α-helix371-3733
β-strand374-37636
β-strand382-38436
α-helix395-3984
β-strand403-40427
α-helix412-4165
α-helix424-43815
α-helix448-45710
α-helix466-4683
α-helix471-48010
α-helix489-4902
α-helix491-4944
α-helix498-5025
α-helix503-5053
α-helix506-5094
α-helix510-51910
Chain C: 24 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix229-23911
α-helix241-2422
α-helix245-2484
β-strand249-25798
β-strand262-26878
β-strand274-28188
α-helix282-2843
α-helix289-30012
β-strand30619
α-helix307-3082
β-strand309-31578
β-strand318-32478
β-strand33019
α-helix331-3377
α-helix342-36120
β-strand364-365210
α-helix371-3733
β-strand374-37639
β-strand382-38439
α-helix387-3893
β-strand391-392210
α-helix393-3942
β-strand404-40527
α-helix407-4093
α-helix412-4154
α-helix423-43816
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-helix510-52011
Chain D: 19 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix231-2399
α-helix2411
α-helix245-2484
β-strand249-257911
β-strand262-268711
β-strand273-281911
α-helix289-30012
β-strand306112
β-strand309-315711
β-strand318-324711
β-strand330112
α-helix331-3377
α-helix342-36120
α-helix371-3733
β-strand374-376312
β-strand382-384312
α-helix395-3984
β-strand403-40424
α-helix412-4165
α-helix423-43816
α-helix448-45811
α-helix466-4683
α-helix471-48010
α-helix489-4902
α-helix491-4944
α-helix498-5025
α-helix503-5053
α-helix506-5094
α-helix510-52011

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
PAK-2p34A, B, C, Dprotein323Homo sapiensQ13177 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9WS6_1 PAK-2p34 (chains A, B, C, D)
MGSSHHHHHHSQDLEVLFQGPHMASMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASG
TVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFV
VMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRNIKSDNVLLGMEGS
VKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP
PYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK
LAKPLSSLTPLIMAAKEAMKSNR

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg4
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32

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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