3Q4Z: Unphosphorylated PAK1 kinase domain

Structure of unphosphorylated PAK1 kinase domain. Determined by X-ray diffraction at 1.89 Å resolution. Released 21 Dec 2011.

Method
X-ray diffraction
Resolution
1.89 Å
Organism
Homo sapiens
Chains
2
Atoms
4,670
Mol. weight
69.56 kDa
Ligands
ANP, MG
Released
21 Dec 2011

Explore 3Q4Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3Q4Z contains 40 α-helices and 22 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: 19 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix252-2609
β-strand27711
β-strand283-28861
β-strand295-30171
α-helix310-32112
β-strand32712
α-helix328-3292
β-strand330-33561
β-strand340-34561
β-strand35112
α-helix352-3587
α-helix363-38220
β-strand385-38623
α-helix392-3943
β-strand395-39732
β-strand403-40532
β-strand412-41323
β-strand42114
α-helix428-4303
α-helix433-4364
β-strand44114
α-helix445-45915
α-helix469-47911
α-helix482-4843
α-helix487-4893
α-helix492-50110
α-helix510-5112
α-helix512-5165
α-helix519-5235
α-helix524-5263
α-helix527-5304
α-helix531-54515
Chain B: 21 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix251-26010
α-helix262-2632
α-helix266-2694
β-strand270-27785
β-strand283-28975
β-strand295-30175
α-helix312-32110
β-strand32716
α-helix328-3292
β-strand330-33675
β-strand339-34575
β-strand35116
α-helix352-3587
α-helix363-38220
α-helix392-3943
β-strand395-39736
β-strand403-40536
α-helix423-4242
α-helix433-4364
α-helix444-45916
α-helix469-47911
α-helix482-4843
α-helix487-4893
α-helix492-50110
α-helix510-5112
α-helix512-5154
α-helix519-5235
α-helix524-5263
α-helix527-5304
α-helix531-54010

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase PAK 1A, Bprotein306Homo sapiensQ13153 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3Q4Z_1 Serine/threonine-protein kinase PAK 1 (chains A, B)
MSDEEILEKLRIIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQP
KKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIA
AVCRECLQALEFLHSNQVIHRNIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT
PYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNP
EKLSAIFRDFLNRCLEMDVEKRGSAKELIQHQFLKIAKPLSSLTPLIAAAKEATKNNHLE
HHHHHH

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31
MGMagnesium ionMg1

Primary citation

Structural insights into the autoactivation mechanism of p21-activated protein kinase. Wang, J., Wu, J.-W., Wang, Z.-X. Structure (2011) 19:1752-1761. DOI 10.1016/j.str.2011.10.013 · PubMed

Other PDB entries of the same protein (UniProt Q13153 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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