4HZS: Ack1 kinase domain with C-terminal SH3 domain

Crystal structure of Ack1 kinase domain with C-terminal SH3 domain. Determined by X-ray diffraction at 3.23 Å resolution. Released 6 Feb 2013.

Method: X-ray diffraction
Resolution: 3.23 Å
Organism: Homo sapiens
Chains: 4
Atoms: 10,196
Mol. weight: 155.45 kDa
Released: 6 Feb 2013

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

Secondary structure: helices and β-sheets

4HZS contains 76 α-helices and 72 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.

Chains A, B and C: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	120	1	1
α-helix	123-125	3
β-strand	126-128	3	1
β-strand	133	1	1
β-strand	139-146	8	1
β-strand	152-159	8	1
α-helix	168-182	15
β-strand	189	1	2
β-strand	192-196	5	1
α-helix	201	1
β-strand	202-205	4	1
β-strand	212	1	2
α-helix	213-219	7
α-helix	226-245	20
α-helix	255-257	3
β-strand	258-260	3	2
β-strand	266-268	3	2
α-helix	273-276	4
α-helix	294-296	3
α-helix	299-304	6
α-helix	309-324	16
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
α-helix	389-391	3
β-strand	392-394	3	3
β-strand	399	1	4
β-strand	407	1	4
β-strand	412-417	6	3
β-strand	419	1	5
β-strand	424-429	6	3
β-strand	435-439	5	3
α-helix	440-443	4

Chain D: 19 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	120	1	15
α-helix	123-125	3
β-strand	126-128	3	15
β-strand	133	1	15
β-strand	139-146	8	15
β-strand	152-159	8	15
α-helix	168-182	15
β-strand	189	1	16
β-strand	192-196	5	15
α-helix	201	1
β-strand	202-205	4	15
β-strand	211-212	2	16
α-helix	213-219	7
α-helix	226-245	20
α-helix	255-257	3
β-strand	258-260	3	16
β-strand	266-268	3	16
α-helix	273-276	4
α-helix	294-296	3
α-helix	299-304	6
α-helix	309-324	16
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
α-helix	389-391	3
β-strand	392-394	3	17
β-strand	399	1	18
β-strand	407	1	18
β-strand	412-417	6	17
β-strand	419	1	14
β-strand	424-429	6	17
β-strand	435-439	5	17
α-helix	440-443	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Activated CDC42 kinase 1	A, B, C, D	protein	341	Homo sapiens	Q07912 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4HZS_1 Activated CDC42 kinase 1 (chains A, B, C, D)
GSQSLTCLIGEKDLRLLEKLGDGSFGVVRRGEWDAPSGKTVSVAVKCLKPDVLSQPEAMD
DFIREVNAMHSLDHRNLIRLYGVVLTPPMKMVTELAPLGSLLDRLRKHQGHFLLGTLSRY
AVQVAEGMGYLESKRFIHRDLAARNLLLATRDLVKIGDFGLMRALPQNDDHYVMQEHRKV
PFAWCAPESLKTRTFSHASDTWMFGVTLWEMFTYGQEPWIGLNGSQILHKIDKEGERLPR
PEDCPQDIYNVMVQCWAHKPEDRPTFVALRDFLLEAQPTDMRALQDFEEPDKLHIQMNDV
ITVIEGRAENYWWRGQNTRTLCVGPFPRNVVTSVAGLSAQD

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:

4HZR 1.31 Å, Crystal structure of Ack1 kinase domain
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…

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