2OFV: Aminoquinazoline 1

crystal structure of aminoquinazoline 1 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: 2
Atoms: 4,211
Mol. weight: 64.96 kDa
Ligands: 242
Released: 27 Feb 2007

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

Secondary structure: helices and β-sheets

2OFV contains 32 α-helices and 20 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: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	239	1	1
α-helix	242-244	3
β-strand	245-254	10	1
β-strand	257-264	8	1
β-strand	268-275	8	1
α-helix	287-294	8
β-strand	300	1	2
α-helix	301-302	2
β-strand	303-307	5	1
β-strand	312-316	5	1
β-strand	323	1	2
α-helix	324-328	5
α-helix	331-334	4
α-helix	338-357	20
α-helix	367-369	3
β-strand	370-372	3	2
β-strand	378-380	3	2
α-helix	409-414	6
α-helix	419-434	16
α-helix	438-439	2
α-helix	446-453	8
α-helix	459-462	4
α-helix	467-476	10
α-helix	481-483	3
α-helix	485-486	2
α-helix	487-495	9

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	236-237	2
β-strand	239	1	3
α-helix	242-244	3
β-strand	245-254	10	3
β-strand	257-264	8	3
β-strand	268-275	8	3
α-helix	286-294	9
β-strand	300	1	4
α-helix	301-302	2
β-strand	303-307	5	3
β-strand	312-316	5	3
β-strand	323	1	4
α-helix	324-327	4
α-helix	338-357	20
α-helix	367-369	3
β-strand	370-372	3	4
β-strand	378-380	3	4
α-helix	404-406	3
α-helix	409-414	6
α-helix	419-433	15
α-helix	438-439	2
α-helix	459-462	4
α-helix	467-476	10
α-helix	481-483	3
α-helix	485-486	2
α-helix	487-495	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Proto-oncogene tyrosine-protein kinase LCK	A, B	protein	277	Homo sapiens	P06239 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2OFV_1 Proto-oncogene tyrosine-protein kinase LCK (chains A, B)
TQKPQKPWWEDEWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAVKSLKQGSMSPDAF
LAEANLMKQLQHQRLVRLYAVVTQEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMA
AQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPIK
WTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMVRPDNC
PEELYQLMRLCWKERPEDRPTFDYLRSVLEDFFTATE

Ligands and cofactors

ID	Name	Formula	Copies
242	3-(2-aminoquinazolin-6-yl)-4-methyl-N-[3-(trifluoromethyl)phenyl]benzamide	C23 H17 F3 N4 O	2

Primary citation

Discovery of Aminoquinazolines as Potent, Orally Bioavailable Inhibitors of Lck: Synthesis, SAR, and in Vivo Anti-Inflammatory Activity. DiMauro, E.F., Newcomb, J., Nunes, J.J. et al. J Med Chem (2006) 49:5671. DOI 10.1021/jm0605482 · 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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