9M41: Serine/threonine-protein kinase PAK 2

The crystal structure of full-length PAK2 containing K278R and D368N mutants. Determined by X-ray diffraction at 3.02 Å resolution. Released 13 Aug 2025.

Method: X-ray diffraction
Resolution: 3.02 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,363
Mol. weight: 121.31 kDa
Ligands: PO4
Released: 13 Aug 2025

Explore 9M41 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9M41 contains 44 α-helices and 27 β-strands across 2 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: 22 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	88-89	2	1
β-strand	95-96	2	1
α-helix	100-108	9
α-helix	113-118	6
α-helix	120-130	11
α-helix	229-235	7
α-helix	236-238	3
β-strand	240-241	2	2
α-helix	245-248	4
β-strand	249-256	8	2
β-strand	262-268	7	2
β-strand	274-281	8	2
α-helix	288-298	11
β-strand	306	1	3
α-helix	307-308	2
β-strand	309-315	7	2
β-strand	318-324	7	2
β-strand	330	1	3
α-helix	331-335	5
α-helix	342-361	20
β-strand	365	1	4
β-strand	374-376	3	3
β-strand	382-384	3	3
β-strand	392	1	4
α-helix	412-415	4
α-helix	423-438	16
α-helix	448-458	11
α-helix	462-464	3
α-helix	466-468	3
α-helix	471-480	10
α-helix	489-490	2
α-helix	491-494	4
α-helix	500-502	3
α-helix	503-505	3
α-helix	506-509	4
α-helix	510-519	10

Chain B: 22 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	87	1	5
β-strand	96	1	5
α-helix	100-107	8
α-helix	113-118	6
α-helix	120-132	13
α-helix	229-235	7
α-helix	240-242	3
α-helix	245-248	4
β-strand	249-256	8	6
β-strand	262-268	7	6
β-strand	274-281	8	6
α-helix	289-298	10
β-strand	306	1	7
α-helix	307-308	2
β-strand	309-315	7	6
β-strand	318-324	7	6
β-strand	330	1	7
α-helix	331-335	5
α-helix	342-361	20
β-strand	365	1	8
β-strand	374-376	3	7
β-strand	382-384	3	7
α-helix	387-389	3
β-strand	392	1	8
α-helix	412-415	4
α-helix	423-438	16
α-helix	448-457	10
α-helix	461-463	3
α-helix	466-468	3
α-helix	471-480	10
α-helix	491-495	5
α-helix	498-502	5
α-helix	503-505	3
α-helix	506-509	4
α-helix	510-519	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase PAK 2	A, B	protein	547	Homo sapiens	Q13177 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9M41_1 Serine/threonine-protein kinase PAK 2 (chains A, B)
MGSSHHHHHHSSGLVPRGSHMASMSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSL
KPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTG
MPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPAL
NAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKS
LDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAI
RQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTE
TCMDEAQIAAVCRECLQALEFLHANQVIHRNIKSDNVLLGMEGSVKLTDFGFCAQITPEQ
SKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAT
NGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAK
EAMKSNR

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	1

Primary citation

Crystal structures of PAK2 reveal new insights into its autoinhibitory mechanism. Hu, H.F., Luo, Z., Zhang, Y. et al. Structure (2025) 33:1663. DOI 10.1016/j.str.2025.07.008 · PubMed

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
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

Browse structure collections

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