8HMT: The complex of ACK1 with the inhibitor 2-142

The complex of ACK1 with the inhibitor 2-142. Determined by X-ray diffraction at 3.17 Å resolution. Released 13 Dec 2023.

Method
X-ray diffraction
Resolution
3.17 Å
Organism
Homo sapiens
Chains
4
Atoms
8,730
Mol. weight
127.26 kDa
Ligands
LWX
Released
13 Dec 2023

Explore 8HMT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8HMT contains 69 α-helices and 56 β-strands across 4 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, 14 β-strands

ElementResiduesLengthSheet
β-strand119-12021
α-helix121-1222
α-helix123-1253
β-strand126-13161
β-strand139-14681
β-strand152-15981
α-helix170-18213
β-strand18912
α-helix190-1912
β-strand192-19651
α-helix2011
β-strand202-20651
β-strand21212
α-helix213-2197
α-helix226-24520
β-strand248-24923
α-helix255-2573
β-strand258-26032
β-strand266-26832
β-strand275-27623
β-strand284-28524
α-helix294-2963
α-helix299-3046
β-strand306-30724
α-helix309-32416
α-helix328-3292
α-helix336-3416
α-helix342-3465
α-helix350-3534
α-helix358-36710
α-helix372-3743
α-helix376-3772
α-helix378-38710
Chain B: 17 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand119-12021
α-helix123-1253
β-strand126-13161
β-strand140-14671
β-strand152-15981
α-helix169-18214
β-strand18915
α-helix190-1912
β-strand192-19651
α-helix2011
β-strand202-20651
β-strand21215
α-helix213-2197
α-helix226-24520
β-strand248-24926
α-helix255-2573
β-strand258-26035
β-strand266-26835
β-strand275-27626
β-strand283-28537
α-helix286-2872
α-helix299-3046
β-strand306-30837
α-helix309-32416
α-helix328-3292
α-helix336-3405
α-helix341-3455
α-helix350-3534
α-helix358-36710
α-helix372-3743
α-helix378-3869
Chain C: 15 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand119-12028
α-helix123-1253
β-strand126-13388
β-strand139-14688
β-strand152-15988
α-helix172-18211
β-strand18919
β-strand192-19658
α-helix2011
β-strand202-20658
β-strand21219
α-helix213-2197
α-helix226-24520
β-strand248-249210
α-helix255-2573
β-strand258-26039
β-strand266-26839
β-strand275-276210
α-helix277-2782
β-strand284-285211
α-helix299-3046
β-strand306-307211
α-helix309-32416
α-helix328-3292
α-helix336-3405
α-helix341-3455
α-helix350-3534
α-helix358-36710
α-helix378-3858
Chain D: 18 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand119-121312
α-helix123-1253
β-strand126-133812
β-strand139-146812
β-strand152-159812
α-helix171-18212
β-strand189113
α-helix190-1912
β-strand192-196512
α-helix2011
β-strand202-206512
β-strand212113
α-helix213-2197
α-helix226-24520
β-strand248-249214
α-helix255-2573
β-strand258-260313
β-strand266-268313
β-strand275-276214
β-strand283-285315
α-helix294-2963
α-helix299-3046
β-strand306-308315
α-helix309-32416
α-helix328-3292
α-helix336-3405
α-helix341-3455
α-helix350-3534
α-helix358-36710
α-helix372-3743
α-helix376-3772
α-helix378-3869

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Activated CDC42 kinase 1A, B, C, Dprotein273Homo sapiensQ07912 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>8HMT_1 Activated CDC42 kinase 1 (chains A, B, C, D)
LTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMDDFIR
EVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRYAVQV
AEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKVPFAW
CAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPRPEDC
PQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQ

Ligands and cofactors

IDNameFormulaCopies
LWX6-(2-bromophenyl)-2-[[3-methyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-8-[[(2S)…C30 H33 Br N6 O24

Primary citation

The complex of ACK1 with the inhibitor 2-142. Zhu, S., Xiaoyun, X.Y. To be published.

Other PDB entries of the same protein (UniProt Q07912 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 8HMT directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.