5XVG: PAK4

Crystal Structure of PAK4 in complex with inhibitor CZH226. Determined by X-ray diffraction at 2.1 Å resolution. Released 7 Feb 2018.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,473
Mol. weight: 33.93 kDa
Ligands: 8FX, EOH
Released: 7 Feb 2018

Explore 5XVG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5XVG contains 23 α-helices and 15 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: 23 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	300-311	12
α-helix	313	1
α-helix	317-319	3
β-strand	321-329	9	1
β-strand	334-340	7	1
β-strand	346-353	8	1
α-helix	354-356	3
α-helix	361-369	9
β-strand	378	1	2
α-helix	379-380	2
β-strand	381-387	7	1
β-strand	390-395	6	1
α-helix	396-398	3
β-strand	401-402	2	2
α-helix	403-409	7
β-strand	410	1	3
α-helix	414-433	20
β-strand	436-437	2	4
α-helix	443-445	3
β-strand	446-448	3	2
β-strand	454-456	3	2
β-strand	463-464	2	4
β-strand	472	1	5
α-helix	479-481	3
α-helix	484-487	4
β-strand	492	1	5
α-helix	495-510	16
α-helix	520-529	10
α-helix	532-533	2
α-helix	538-540	3
α-helix	543-552	10
α-helix	561-562	2
α-helix	563-566	4
α-helix	570-574	5
α-helix	575-577	3
α-helix	578-581	4
α-helix	582-585	4
β-strand	589	1	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase PAK 4	A	protein	293	Homo sapiens	O96013 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5XVG_1 Serine/threonine-protein kinase PAK 4 (chains A)
SSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQ
RRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIA
AVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGT
PYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNL
HKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR

Ligands and cofactors

ID	Name	Formula	Copies
8FX	[6-chloranyl-4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl]-[(3R)-3-m…	C20 H22 Cl N7 O	1
EOH	Ethanol	C2 H6 O	5

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

Primary citation

Structure-Based Design of 6-Chloro-4-aminoquinazoline-2-carboxamide Derivatives as Potent and Selective p21-Activated Kinase 4 (PAK4) Inhibitors. Hao, C., Zhao, F., Song, H. et al. J Med Chem (2018) 61:265-285. DOI 10.1021/acs.jmedchem.7b01342 · PubMed

Other PDB entries of the same protein (UniProt O96013 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2J0I 1.6 Å, Crystal structure of the human P21-activated kinase 4
2Q0N 1.75 Å, Structure of human p21 activating kinase 4 (PAK4) in complex with a consensus peptide
5VEF 1.75 Å, PAK4 kinase domain in complex with fasudil
5ZJW 1.8 Å, Crystal Structure of PAK4 in complex with inhibitor CZg353
5XVA 1.85 Å, Crystal Structure of PAK4 in complex with inhibitor CZH216
4JDI 1.85 Å, Crystal structure of Serine/threonine-protein kinase PAK 4 in complex with Paktide S…
8AHG 1.89 Å, PAC-FragmentDEL: Photoactivated covalent capture of DNA encoded fragments for hit…
6WLY 1.9 Å, PAK4 kinase domain in complex with LIMK1 Thr508 substrate peptide
7S48 1.9 Å, PAK4cat in complex with Integrin beta5 760-770 peptide
4FIH 1.97 Å, Catalytic domain of human PAK4 with QKFTGLPRQW peptide
4FII 2.0 Å, Catalytic domain of human PAK4 with RPKPLVDP peptide
4JDH 2.0 Å, Crystal structure of Serine/threonine-protein kinase PAK 4 in complex with Paktide T…

Browse structure collections

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