2OFU: 2-aminopyrimidine carbamate 43

x-ray crystal structure of 2-aminopyrimidine carbamate 43 bound to Lck. Determined by X-ray diffraction at 2.0 Å resolution. Released 27 Feb 2007.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,575
Mol. weight: 32.43 kDa
Ligands: 1N9
Released: 27 Feb 2007

Explore 2OFU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OFU contains 16 α-helices and 16 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: 16 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	230-232	3
β-strand	239	1	1
α-helix	242-244	3
β-strand	245-253	9	1
β-strand	257-264	8	1
β-strand	268-275	8	1
β-strand	277	1	2
β-strand	280	1	2
α-helix	282-294	13
β-strand	300	1	3
α-helix	301-302	2
β-strand	303-307	5	1
β-strand	313-317	5	1
β-strand	323	1	3
α-helix	324-327	4
α-helix	331-334	4
α-helix	338-357	20
β-strand	360-361	2	4
α-helix	367-369	3
β-strand	370-372	3	3
β-strand	378-380	3	3
β-strand	387-388	2	4
β-strand	394-395	2	5
α-helix	409-414	6
β-strand	416-417	2	5
α-helix	419-434	16
α-helix	438-439	2
α-helix	446-454	9
α-helix	459-462	4
α-helix	467-476	10
α-helix	481-483	3
α-helix	487-500	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proto-oncogene tyrosine-protein kinase LCK	A	protein	273	Homo sapiens	P06239 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2OFU_1 Proto-oncogene tyrosine-protein kinase LCK (chains A)
PQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAFLAE
ANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQI
AEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIKWTA
PEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNCPEE
LYQLMRLCWKERPEDRPTFDYLRSVLEDFFTAT

Ligands and cofactors

ID	Name	Formula	Copies
1N9	2,6-dimethylphenyl 2-(3,5-dimethoxy-4-(3-(4-methylpiperazin-1-yl)propoxy)phenyl…	C37 H46 N6 O7	1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Novel 2-Aminopyrimidine Carbamates as Potent and Orally Active Inhibitors of Lck: Synthesis, SAR, and in Vivo Antiinflammatory Activity. Martin, M.W., Newcomb, J., Nunes, J.J. et al. J Med Chem (2006) 49:4981. DOI 10.1021/jm060435i · PubMed

Other PDB entries of the same protein (UniProt P06239 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LKK 1.0 Å, Human P56-lck tyrosine kinase SH2 domain in complex with the phosphotyrosyl peptide…
2IIM 1.0 Å, SH3 Domain of Human Lck
8X2P 1.4 Å, The Crystal Structure of LCK from Biortus.
1QPC 1.6 Å, Structural analysis of the lymphocyte-specific kinase lck in complex with non-selective…
3LCK 1.7 Å, The kinase domain of human lymphocyte kinase (LCK), activated form (auto-phosphorylated…
4C3F 1.72 Å, Structure of Lck in complex with a compound discovered by Virtual Fragment Linking
1BHF 1.8 Å, P56LCK SH2 domain inhibitor complex
1LCJ 1.8 Å, SH2 (src homology-2) domain of human P56-lck tyrosine kinase complexed with the 11…
1LKL 1.8 Å, Human P56-lck tyrosine kinase SH2 domain in complex with the phosphotyrosyl peptide…
6PDJ 1.81 Å, Tyrosine-protein kinase LCK bound to Compound 11
1BHH 1.9 Å, Free P56LCK SH2 domain
3MPM 1.95 Å, LCK complexed with a pyrazolopyrimidine

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