4FII: Serine/threonine-protein kinase PAK 4

Catalytic domain of human PAK4 with RPKPLVDP peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Sept 2012.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,542
Mol. weight: 40.05 kDa
Released: 12 Sept 2012

Explore 4FII in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FII contains 22 α-helices and 17 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: 21 helices, 16 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	360-363	4
α-helix	364-372	9
β-strand	378	1	2
β-strand	381-387	7	1
β-strand	390-395	6	1
β-strand	401-402	2	2
α-helix	403-407	5
α-helix	414-433	20
β-strand	436-437	2	3
α-helix	443-445	3
β-strand	446-448	3	2
β-strand	454-456	3	2
α-helix	459-461	3
β-strand	463-464	2	3
β-strand	466	1	4
β-strand	469	1	4
β-strand	472	1	5
β-strand	477	1	6
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	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	578-580	3
α-helix	582-584	3

Chain B: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	50-52	3
β-strand	53	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein kinase PAK 4	A	protein	346	Homo sapiens	O96013 (AlphaFold model)
Serine/threonine-protein kinase PAK 4	B	protein	8	Homo sapiens	O96013 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4FII_1 Serine/threonine-protein kinase PAK 4 (chains A)
MGSSHHHHHHSSGLVPRGSHMENLYFQGARARQENGMPEKPPGPRSPQREPQRVSHEQFR
AALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFN
EVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVL
QALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPE
LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSL
KGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR

Sequence of entity 2 (B), FASTA

>4FII_2 Serine/threonine-protein kinase PAK 4 (chains B)
RPKPLVDP

Primary citation

Type II p21-activated kinases (PAKs) are regulated by an autoinhibitory pseudosubstrate. Ha, B.H., Davis, M.J., Chen, C. et al. Proc Natl Acad Sci U S A (2012) 109:16107-16112. DOI 10.1073/pnas.1214447109 · 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
4JDH 2.0 Å, Crystal structure of Serine/threonine-protein kinase PAK 4 in complex with Paktide T…
7S47 2.0 Å, Integrin beta5(743-774)-linker-PAK4cat(D440N/S474E)

Browse structure collections

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