3CS9: Human ABL kinase

Human ABL kinase in complex with nilotinib. Determined by X-ray diffraction at 2.21 Å resolution. Released 22 Apr 2008.

Method: X-ray diffraction
Resolution: 2.21 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,696
Mol. weight: 130.32 kDa
Ligands: NIL
Released: 22 Apr 2008

Explore 3CS9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3CS9 contains 80 α-helices and 44 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: 21 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	236	1	1
α-helix	239-241	3
β-strand	242-247	6	1
α-helix	248-251	4
β-strand	256-261	6	1
α-helix	262-264	3
β-strand	266-272	7	1
α-helix	280-291	12
β-strand	298	1	2
α-helix	299-300	2
β-strand	301-305	5	1
α-helix	311	1
β-strand	312-316	5	1
β-strand	321-322	2	2
α-helix	323-329	7
α-helix	337-356	20
α-helix	366-368	3
β-strand	369-371	3	2
α-helix	373-375	3
β-strand	377-379	3	2
α-helix	384-386	3
β-strand	394-396	3	3
β-strand	399-401	3	3
α-helix	403-405	3
α-helix	408-413	6
α-helix	418-433	16
α-helix	437-438	2
α-helix	445-453	9
α-helix	458-461	4
α-helix	466-475	10
α-helix	480-482	3
α-helix	484-485	2
α-helix	486-498	13

Chain B: 21 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	236	1	4
α-helix	239-241	3
β-strand	242-247	6	4
α-helix	249-251	3
β-strand	256-261	6	4
α-helix	262-264	3
β-strand	266-272	7	4
α-helix	280-292	13
β-strand	298	1	5
α-helix	299-300	2
β-strand	301-305	5	4
α-helix	311	1
β-strand	312-316	5	4
β-strand	322	1	5
α-helix	323-329	7
α-helix	337-356	20
α-helix	366-368	3
β-strand	369-371	3	5
α-helix	373-375	3
β-strand	377-379	3	5
α-helix	403-405	3
α-helix	408-413	6
α-helix	418-433	16
α-helix	437-438	2
α-helix	445-447	3
α-helix	448-453	6
α-helix	458-461	4
α-helix	466-475	10
α-helix	480-482	3
α-helix	484-485	2
α-helix	486-499	14

Chain C: 20 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	236	1	6
α-helix	239-241	3
β-strand	242-247	6	6
α-helix	250-253	4
β-strand	256-261	6	6
α-helix	262-264	3
β-strand	266-271	6	6
α-helix	280-292	13
β-strand	298	1	7
α-helix	299-300	2
β-strand	301-305	5	6
α-helix	311	1
β-strand	312-316	5	6
β-strand	322	1	7
α-helix	323-329	7
α-helix	337-356	20
α-helix	366-368	3
β-strand	369-371	3	7
α-helix	373-375	3
β-strand	377-379	3	7
α-helix	403-405	3
α-helix	408-413	6
α-helix	418-433	16
α-helix	437-438	2
α-helix	445-453	9
α-helix	459-461	3
α-helix	466-475	10
α-helix	480-482	3
α-helix	484-485	2
α-helix	486-496	11

Chain D: 18 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	236	1	8
α-helix	239-241	3
β-strand	243-247	5	8
α-helix	248-251	4
β-strand	256-260	5	8
β-strand	268-273	6	8
α-helix	279-291	13
β-strand	298	1	9
α-helix	299-300	2
β-strand	301-305	5	8
β-strand	311-316	6	8
β-strand	322	1	9
α-helix	323-329	7
α-helix	337-356	20
α-helix	366-368	3
β-strand	369-371	3	9
α-helix	373-375	3
β-strand	377-379	3	9
α-helix	384-387	4
β-strand	394-396	3	10
β-strand	399-401	3	10
α-helix	403-405	3
α-helix	408-413	6
α-helix	418-433	16
α-helix	437-438	2
α-helix	445-453	9
α-helix	458-461	4
α-helix	466-474	9
α-helix	484-485	2
α-helix	486-497	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proto-oncogene tyrosine-protein kinase ABL1	A, B, C, D	protein	277	Homo sapiens	P00519 (AlphaFold model)

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

>3CS9_1 Proto-oncogene tyrosine-protein kinase ABL1 (chains A, B, C, D)
GAMDPSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEEF
LKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQEVNAVVLLYM
ATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKFPI
KWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEG
CPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQES

Ligands and cofactors

ID	Name	Formula	Copies
NIL	Nilotinib	C28 H22 F3 N7 O	4

Primary citation

Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl. Weisberg, E., Manley, P.W., Breitenstein, W. et al. Cancer Cell (2005) 7:129-141. DOI 10.1016/j.ccr.2005.01.007 · PubMed

Other PDB entries of the same protein (UniProt P00519 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5OAZ 1.03 Å, Crystal structure of the Abl-SH3 domain at pH 7.5
7PVS 1.05 Å, Crystal structure of the Abl SH3 domain V73E-A74S-S75R-G76T-D77E-G92N-Y93N-N94T-H95E…
4J9C 1.05 Å, Crystal structure of the Abl-SH3 domain H59Q-N96T mutant complexed with the designed…
4J9F 1.09 Å, Crystal structure of the Abl-SH3 domain complexed with the high affinity peptide P0
7PW2 1.1 Å, Crystal structure of the Abl SH3 domain V73E-A74S-S75R-G76T-D77E mutant
3EG3 1.4 Å, Crystal structure of the N114A mutant of ABL-SH3 domain
4J9E 1.4 Å, Crystal structure of the N114A mutant of the Abl-SH3 domain complexed with the high…
5DC4 1.48 Å, Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal a
4J9D 1.5 Å, Crystal structure of the N114A mutant of the Abl-SH3 domain complexed with the high…
5HU9 1.53 Å, Crystal structure of ABL1 in complex with CHMFL-074
7PVQ 1.55 Å, Crystal structure of the Abl SH3 domain V73E-A74S-S75R-G76T-D77E-G92N-Y93N-N94T-H95E…
5DC9 1.56 Å, Crystal structure of monobody AS25/ABL1 SH2 domain complex, crystal B

Browse more

3CS9 is part of these collections:

Kinases and cancer drug targets

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