4HZR: Ack1 kinase domain

Crystal structure of Ack1 kinase domain. Determined by X-ray diffraction at 1.31 Å resolution. Released 6 Feb 2013.

Method: X-ray diffraction
Resolution: 1.31 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,766
Mol. weight: 63.52 kDa
Released: 6 Feb 2013

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

Secondary structure: helices and β-sheets

4HZR contains 42 α-helices and 28 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, 14 β-strands

Element	Residues	Length	Sheet
β-strand	119-120	2	1
α-helix	123-125	3
β-strand	126-133	8	1
β-strand	140-146	7	1
β-strand	152-159	8	1
α-helix	171-181	11
β-strand	189	1	2
α-helix	190-191	2
β-strand	192-196	5	1
α-helix	201	1
β-strand	202-206	5	1
β-strand	212	1	2
α-helix	213-219	7
α-helix	221-223	3
α-helix	226-245	20
β-strand	248-249	2	3
α-helix	255-257	3
β-strand	258-262	5	2
β-strand	265-268	4	2
β-strand	275-276	2	3
α-helix	277-278	2
β-strand	284-285	2	4
α-helix	286-287	2
α-helix	294-296	3
α-helix	299-304	6
β-strand	306-307	2	4
α-helix	309-324	16
α-helix	328-329	2
α-helix	336-340	5
α-helix	341-345	5
α-helix	350-353	4
α-helix	358-367	10
α-helix	372-374	3
α-helix	376-377	2
α-helix	378-387	10

Chain B: 21 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	119-120	2	1
α-helix	123-125	3
β-strand	126-131	6	1
β-strand	140-146	7	1
β-strand	152-158	7	1
α-helix	170-181	12
β-strand	189	1	5
α-helix	190-191	2
β-strand	192-196	5	1
α-helix	201	1
β-strand	202-206	5	1
β-strand	212	1	5
α-helix	213-220	8
α-helix	221-223	3
α-helix	226-245	20
β-strand	248-249	2	6
α-helix	255-257	3
β-strand	258-262	5	5
β-strand	265-268	4	5
β-strand	275-276	2	6
α-helix	277-278	2
β-strand	284-285	2	7
α-helix	286-287	2
α-helix	294-296	3
α-helix	299-304	6
β-strand	306-307	2	7
α-helix	309-324	16
α-helix	328-329	2
α-helix	336-340	5
α-helix	341-345	5
α-helix	350-353	4
α-helix	358-367	10
α-helix	372-374	3
α-helix	376-377	2
α-helix	378-388	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Activated CDC42 kinase 1	A, B	protein	277	Homo sapiens	Q07912 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4HZR_1 Activated CDC42 kinase 1 (chains A, B)
GSQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMD
DFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRY
AVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKV
PFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPR
PEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQ

Primary citation

Ack1: activation and regulation by allostery. Gajiwala, K.S., Maegley, K., Ferre, R. et al. PLoS One (2013) 8:e53994-e53994. DOI 10.1371/journal.pone.0053994 · PubMed

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

8THA 1.68 Å, 1TEL, non-compressed, double-helical crystal form
7KP6 1.79 Å, Structure of Ack1 kinase in complex with a selective inhibitor
8Q5P 1.81 Å, Structure of the lysine methyltransferase SETD2 in complex with a peptide derived from…
1U46 2.0 Å, Crystal Structure of the Unphosphorylated Kinase Domain of the Tyrosine Kinase ACK1
3EQR 2.0 Å, Crystal Structure of Ack1 with compound T74
1U4D 2.1 Å, Structure of the ACK1 Kinase Domain bound to Debromohymenialdisine
5ZXB 2.2 Å, Crystal structure of ACK1 with compound 10d
3EQP 2.3 Å, Crystal Structure of Ack1 with compound T95
4EWH 2.5 Å, Co-crystal structure of ACK1 with inhibitor
8FZ3 2.78 Å, Sterile Alpha Motif of Human Translocation ETS Leukemia, Non-Polymer Crystal Form
1U54 2.8 Å, Crystal Structures of the Phosphorylated and Unphosphorylated Kinase Domains of the…
6VQM 2.87 Å, Crystal Structure Analysis of human ACK1

Browse structure collections

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