2C30: Human P21-Activated Kinase 6

Crystal Structure Of The Human P21-Activated Kinase 6. Determined by X-ray diffraction at 1.6 Å resolution. Released 8 Feb 2006.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
2,691
Mol. weight
36.81 kDa
Ligands
PO4
Released
8 Feb 2006

Explore 2C30 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2C30 contains 19 α-helices and 13 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: 19 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix387-3959
α-helix3991
α-helix403-4064
β-strand407-416101
β-strand419-42681
β-strand432-43981
α-helix446-45611
β-strand46412
β-strand467-47371
β-strand476-48161
β-strand48812
α-helix489-4935
α-helix500-51920
β-strand522-52323
α-helix529-5313
β-strand532-53432
β-strand540-54232
β-strand549-55023
β-strand55814
α-helix565-5673
α-helix570-5734
β-strand57814
α-helix581-59616
α-helix606-61510
α-helix618-6192
α-helix624-6263
α-helix629-63810
α-helix647-6482
α-helix649-6535
α-helix656-6605
α-helix664-6674
α-helix668-6736

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase pak 6Aprotein321HOMO SAPIENSQ9NQU5 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2C30_1 SERINE/THREONINE-PROTEIN KINASE PAK 6 (chains A)
MHHHHHHSSGVDLGTENLYFQSGVVTHEQFKAALRMVVDQGDPRLLLDSYVKIGEGSTGI
VCLAREKHSGRQVAVKMMDLRKQQRRELLFNEVVIMRDYQHFNVVEMYKSYLVGEELWVL
MEFLQGGALTDIVSQVRLNEEQIATVCEAVLQALAYLHAQGVIHRDIKSDSILLTLDGRV
KLSDFGFCAQISKDVPKRKSLVGTPYWMAPEVISRSLYATEVDIWSLGIMVIEMVDGEPP
YFSDSPVQAMKRLRDSPPPKLKNSHKVSPVLRDFLERMLVRDPQERATAQELLDHPFLLQ
TGLPECLVPLIQLYRKQTSTC

Ligands and cofactors

IDNameFormulaCopies
PO4Phosphate ionO4 P1

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

Primary citation

Crystal Structures of the P21-Activated Kinases Pak4, Pak5, and Pak6 Reveal Catalytic Domain Plasticity of Active Group II Paks. Eswaran, J., Lee, W.H., Debreczeni, J.E. et al. Structure (2007) 15:201. DOI 10.1016/J.STR.2007.01.001 · PubMed

Other PDB entries of the same protein (UniProt Q9NQU5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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