3POZ: EGFR Kinase domain

EGFR Kinase domain complexed with tak-285. Determined by X-ray diffraction at 1.5 Å resolution. Released 30 Mar 2011.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,536
Mol. weight: 38.14 kDa
Ligands: 03P
Released: 30 Mar 2011

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

Secondary structure: helices and β-sheets

3POZ contains 21 α-helices and 13 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: 21 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	705-706	2	1
α-helix	709-711	3
β-strand	712-721	10	1
β-strand	724-731	8	1
β-strand	740-746	7	1
α-helix	756-768	13
β-strand	771	1	2
β-strand	774	1	2
β-strand	777-782	6	1
β-strand	786-791	6	1
β-strand	797	1	2
α-helix	798-804	7
α-helix	811-830	20
α-helix	840-842	3
β-strand	843-847	5	2
β-strand	850-853	4	2
α-helix	858-862	5
α-helix	878-880	3
α-helix	883-888	6
α-helix	893-908	16
α-helix	912-913	2
α-helix	920-922	3
α-helix	923-928	6
α-helix	933-936	4
β-strand	939	1	3
α-helix	941-950	10
α-helix	955-957	3
α-helix	959-960	2
α-helix	961-972	12
α-helix	975-978	4
β-strand	979	1	3
α-helix	984-986	3
α-helix	996-1002	7
α-helix	1013-1016	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Epidermal growth factor receptor	A	protein	327	Homo sapiens	P00533 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3POZ_1 Epidermal growth factor receptor (chains A)
GEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKA
NKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLL
NWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGK
VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQ
PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDS
NFYRALMDEEDMDDVVDADEYLIPQQG

Ligands and cofactors

ID	Name	Formula	Copies
03P	N-{2-[4-({3-chloro-4-[3-(trifluoromethyl)phenoxy]phenyl}amino)-5H-pyrrolo[3,2-d…	C26 H25 Cl F3 N5 O3	1

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

Primary citation

Structural Analysis of the Mechanism of Inhibition and Allosteric Activation of the Kinase Domain of HER2 Protein. Aertgeerts, K., Skene, R., Yano, J. et al. J Biol Chem (2011) 286:18756-18765. DOI 10.1074/jbc.M110.206193 · PubMed

Other PDB entries of the same protein (UniProt P00533 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8A27 1.07 Å, EGFR kinase domain in complex with 2-(6,7-dihydro-5H-pyrrolo[1,2-c]imidazol-1-yl)-2-[6-[2…
8A2D 1.11 Å, EGFR kinase domain (L858R/V948R) in complex with 2-[4-(difluoromethyl)-6-[2-[4-[[4-(hydro…
5UG9 1.33 Å, Crystal structure of the EGFR kinase domain (L858R, T790M, V948R) in complex with a…
5HG8 1.42 Å, EGFR (L858R, T790M, V948R) in complex with N-[3-({2-[(1-methyl-1H-pyrazol-4-yl)amino]-7H-…
8A2A 1.43 Å, EGFR kinase domain in complex with 2-(6,7-dihydro-5H-pyrrolo[1,2-c]imidazol-1-yl)-2-[6-[2…
5UG8 1.46 Å, Crystal structure of the EGFR kinase domain (L858R, T790M, V948R) in complex with a…
6TFV 1.5 Å, Crystal Structure of EGFR T790M/V948R in Complex with Covalent Pyrrolopyrimidine 18b
6TG0 1.5 Å, Crystal Structure of EGFR T790M/V948R in Complex with Covalent Pyrrolopyrimidine 21a
3VRP 1.52 Å, Crystal structure of the tyrosine kinase binding domain of Cbl-c in complex with…
5HG5 1.52 Å, EGFR (L858R, T790M, V948R) in complex with N-{3-[(2-{[4-(4-methylpiperazin-1-yl)phenyl]am…
5CNO 1.55 Å, Crystal structure of the EGFR kinase domain mutant V924R
9NTP 1.55 Å, EGFR kinase domain (T790MV948R) in complex with a strain-release covalent inhibitor

Browse structure collections

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