9WS5: PAK2 kinase domain containing D368N mutant

Crystal structure of PAK2 kinase domain containing D368N mutant. Determined by X-ray diffraction at 2.4 Å resolution. Released 16 Sept 2026.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,115
Mol. weight: 36.72 kDa
Ligands: CIT
Released: 16 Sept 2026

Explore 9WS5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WS5 contains 19 α-helices and 9 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: 19 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	229-236	8
α-helix	245-248	4
β-strand	249-258	10	1
β-strand	261-268	8	1
β-strand	274-281	8	1
α-helix	288-300	13
β-strand	306	1	2
α-helix	307-308	2
β-strand	309-315	7	1
β-strand	318-324	7	1
β-strand	330	1	2
α-helix	331-337	7
α-helix	342-361	20
α-helix	371-373	3
β-strand	374-376	3	2
β-strand	382-384	3	2
α-helix	424-438	15
α-helix	440	1
α-helix	442	1
α-helix	443-446	4
α-helix	448-456	9
α-helix	460-464	5
α-helix	471-480	10
α-helix	489-490	2
α-helix	491-494	4
α-helix	498-502	5
α-helix	506-509	4
α-helix	510-521	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PAK-2p34	A	protein	323	Homo sapiens	Q13177 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9WS5_1 PAK-2p34 (chains A)
MGSSHHHHHHSQDLEVLFQGPHMADLTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASG
TVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFV
VMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRNIKSDNVLLGMEGS
VKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEP
PYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLK
LAKPLSSLTPLIMAAKEAMKSNR

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	2

Water and common crystallization additives (SO4) 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:

9WS3 1.85 Å, Crystal structure of phosphorylated PAK2 kinase domain containing K278R mutant
9WS2 1.9 Å, Crystal structure of nucleotide-bound PAK2 kinase domain containing K278R mutant
9WS6 2.0 Å, Crystal structure of AMP-PNP-bound PAK2 kinase domain containing D368N mutant
9D51 2.1 Å, Structure of PAK2 in complex with compound 12
9LBF 2.62 Å, The crystal structure of the truncated PAK2 containing D368N mutant
3PCS 2.86 Å, Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex
9LBG 2.89 Å, The crystal structure of the truncated PAK2 containing K278R mutant
9M41 3.02 Å, The crystal structure of full-length PAK2 containing K278R and D368N mutants

Browse structure collections

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