9WS2: PAK-2p34

Crystal structure of nucleotide-bound PAK2 kinase domain containing K278R mutant. Determined by X-ray diffraction at 1.9 Å resolution. Released 16 Sept 2026.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,678
Mol. weight: 35.53 kDa
Ligands: GAI, ANP
Released: 16 Sept 2026

Explore 9WS2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9WS2 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

Element	Residues	Length	Sheet
α-helix	229-236	8
β-strand	240	1	1
α-helix	245-248	4
β-strand	249-258	10	1
β-strand	261-268	8	1
β-strand	273-281	9	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	331-335	5
α-helix	342-361	20
β-strand	364-365	2	3
α-helix	371-373	3
β-strand	374-376	3	2
β-strand	382-384	3	2
β-strand	391-392	2	3
β-strand	400	1	4
α-helix	407-409	3
α-helix	412-415	4
β-strand	420	1	4
α-helix	424-438	15
α-helix	448-458	11
α-helix	461-463	3
α-helix	466-468	3
α-helix	471-480	10
α-helix	489-490	2
α-helix	491-494	4
α-helix	498-502	5
α-helix	503-505	3
α-helix	506-509	4
α-helix	510-525	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PAK-2p34	A	protein	309	Homo sapiens	Q13177 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9WS2_1 PAK-2p34 (chains A)
MASMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIRQINLQ
KQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEA
QIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTM
VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPEL
QNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSN
RLEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
GAI	Guanidine	C H5 N3	1
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	1

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:

9WS3 1.85 Å, Crystal structure of phosphorylated 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
9WS5 2.4 Å, Crystal structure of PAK2 kinase domain containing D368N mutant
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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