1OPK: The auto-inhibition of c-Abl tyrosine kinase

Structural basis for the auto-inhibition of c-Abl tyrosine kinase. Determined by X-ray diffraction at 1.8 Å resolution. Released 8 Apr 2003.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Mus musculus
Chains
1
Atoms
3,933
Mol. weight
56.94 kDa
Ligands
MYR, P16
Released
8 Apr 2003

Explore 1OPK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OPK contains 30 α-helices and 34 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: 30 helices, 34 β-strands

ElementResiduesLengthSheet
β-strand84-8741
β-strand9112
β-strand9811
β-strand10112
β-strand106-11271
β-strand118-12251
β-strand127-13151
α-helix132-1343
β-strand135-13731
α-helix141-1433
β-strand147-15043
α-helix153-1597
α-helix160-1623
β-strand167-17263
β-strand180-18673
β-strand189-19463
α-helix1951
β-strand196-19724
β-strand203-20424
β-strand21114
α-helix214-2218
β-strand22615
β-strand22815
β-strand234-23523
α-helix236-2372
α-helix241-2433
β-strand25516
α-helix258-2603
β-strand261-26666
α-helix268-2703
β-strand275-28066
α-helix281-2833
β-strand285-29176
α-helix299-31113
β-strand31717
β-strand320-32456
α-helix3301
β-strand331-33556
β-strand34117
α-helix342-3487
α-helix356-37520
β-strand378-37928
α-helix385-3873
β-strand388-39037
α-helix392-3943
β-strand396-39837
β-strand404-40528
β-strand40819
β-strand41019
β-strand412-413210
α-helix414-4152
α-helix422-4243
α-helix427-4326
β-strand434-435210
α-helix437-45216
α-helix456-4572
α-helix464-4663
α-helix467-4726
α-helix477-4804
α-helix485-49410
α-helix499-5013
α-helix503-5042
α-helix505-5139
α-helix521-53010

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proto-oncogene tyrosine-protein kinase ABL1Aprotein495Mus musculusP00520 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1OPK_1 Proto-oncogene tyrosine-protein kinase ABL1 (chains A)
GAMDPSEALQRPVASDFEPQGLSEAARWNSKENLLAGPSENDPNLFVALYDFVASGDNTL
SITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPVNSLEKHSWYHGPVSRNAAEYL
LSSGINGSFLVRESESSPGQRSISLRYEGRVYHYRINTASDGKLYVSSESRFNTLAELVH
HHSTVADGLITTLHYPAPKRNKPTIYGVSPNYDKWEMERTDITMKHKLGGGQYGEVYEGV
WKKYSLTVAVKTLKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTY
GNLLDYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRNLAARNCLVGENHLVKVA
DFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPY
PGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRPSFAEIHQAFETMFQES
SISDEVEKELGKRGT

Ligands and cofactors

IDNameFormulaCopies
MYRMyristic acidC14 H28 O21
P166-(2,6-dichlorophenyl)-2-{[3-(hydroxymethyl)phenyl]amino}-8-METHYLPYRIDO[2,3-D]…C21 H16 Cl2 N4 O21

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

Primary citation

Structural basis for the autoinhibition of c-Abl tyrosine kinase. Nagar, B., Hantschel, O., Young, M.A. et al. Cell (2003) 112:859-871. DOI 10.1016/S0092-8674(03)00194-6 · PubMed

Other PDB entries of the same protein (UniProt P00520 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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