9LBG: Truncated PAK2 containing K278R mutant

The crystal structure of the truncated PAK2 containing K278R mutant. Determined by X-ray diffraction at 2.89 Å resolution. Released 13 Aug 2025.

Method: X-ray diffraction
Resolution: 2.89 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,426
Mol. weight: 103.68 kDa
Ligands: MLT
Released: 13 Aug 2025

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

Secondary structure: helices and β-sheets

9LBG contains 43 α-helices and 23 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: 23 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	89	1	1
β-strand	94	1	1
α-helix	100-107	8
α-helix	113-118	6
α-helix	120-130	11
α-helix	229-235	7
α-helix	236-238	3
β-strand	241	1	2
α-helix	245-248	4
β-strand	249-251	3	2
β-strand	252	1	3
β-strand	253-258	6	2
β-strand	261-268	8	2
β-strand	274-281	8	2
α-helix	288-300	13
β-strand	306	1	4
α-helix	307-308	2
β-strand	309-315	7	2
β-strand	318-324	7	2
β-strand	330	1	4
α-helix	331-337	7
α-helix	342-361	20
α-helix	371-373	3
β-strand	374-376	3	4
β-strand	382-384	3	4
α-helix	412-415	4
α-helix	423-438	16
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	510-520	11

Chain B: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	95	1
α-helix	103-108	6
α-helix	113-118	6
α-helix	120-131	12
α-helix	229-235	7
α-helix	245-248	4
β-strand	249-258	10	5
β-strand	261-268	8	5
β-strand	273-281	9	5
α-helix	288-298	11
β-strand	306	1	6
β-strand	309-315	7	5
β-strand	318-324	7	5
β-strand	330	1	6
α-helix	331-337	7
α-helix	342-361	20
α-helix	371-373	3
β-strand	374-376	3	6
β-strand	382-384	3	6
α-helix	412-415	4
α-helix	424-438	15
α-helix	448-457	10
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	510-519	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase PAK 2	A, B	protein	466	Homo sapiens	Q13177 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9LBG_1 Serine/threonine-protein kinase PAK 2 (chains A, B)
MGSSHHHHHHSSGLVPRGSHMASHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKK
NPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEET
APPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRT
IVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIRQINLQKQPKKELIINEILVM
KELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEF
LHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRK
AYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLN
RCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR

Ligands and cofactors

ID	Name	Formula	Copies
MLT	D-malate	C4 H6 O5	1

Water and common crystallization additives (SO4) are not listed.

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
9M41 3.02 Å, The crystal structure of full-length PAK2 containing K278R and D368N mutants

Browse structure collections

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