4ZSA: FGFR1 kinase domain

Crystal structure of FGFR1 kinase domain in complex with 7n. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Jun 2015.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,850
Mol. weight: 71.07 kDa
Ligands: 4UT
Released: 17 Jun 2015

Explore 4ZSA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ZSA 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	472	1	1
α-helix	475-477	3
β-strand	478-484	7	1
β-strand	491-498	8	1
β-strand	508-515	8	1
α-helix	522-538	17
β-strand	544	1	2
β-strand	547-551	5	1
β-strand	558-562	5	1
β-strand	568	1	2
α-helix	569-574	6
α-helix	593-596	4
α-helix	597-616	20
α-helix	626-628	3
β-strand	629-631	3	2
β-strand	637-639	3	2
α-helix	663-666	4
α-helix	669-674	6
α-helix	679-694	16
α-helix	698-699	2
α-helix	706-714	9
α-helix	719-722	4
α-helix	727-736	10
α-helix	741-743	3
α-helix	745-746	2
α-helix	747-760	14

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	472	1	3
α-helix	475-477	3
β-strand	478-483	6	3
α-helix	485-487	3
β-strand	492-498	7	3
β-strand	508-514	7	3
α-helix	522-538	17
β-strand	544	1	4
β-strand	547-551	5	3
β-strand	558-562	5	3
β-strand	568	1	4
α-helix	569-574	6
α-helix	597-616	20
α-helix	626-628	3
β-strand	629-631	3	4
β-strand	637-639	3	4
α-helix	663-666	4
α-helix	669-673	5
α-helix	679-694	16
α-helix	698-699	2
α-helix	706-714	9
α-helix	719-722	4
α-helix	727-736	10
α-helix	741-743	3
α-helix	745-746	2
α-helix	747-759	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibroblast growth factor receptor 1	A, B	protein	308	Homo sapiens	P11362 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4ZSA_1 Fibroblast growth factor receptor 1 (chains A, B)
AGVSEYELPEDPRWELPRDRLVLGKPLGEGAFGQVVLAEAIGLDKDKPNRVTKVAVKMLK
SDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARR
PPGLEYSYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVM
KIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLG
GSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRI
VALTSNQE

Ligands and cofactors

ID	Name	Formula	Copies
4UT	4-(4-ethylpiperazin-1-yl)-N-[6-(3-methoxyphenyl)-2H-indazol-3-yl]benzamide	C27 H29 N5 O2	2

Primary citation

Design, synthesis and biological evaluation of novel FGFR inhibitors bearing an indazole scaffold. Liu, J., Peng, X., Dai, Y. et al. Org Biomol Chem (2015) 13:7643-7654. DOI 10.1039/c5ob00778j · PubMed

Other PDB entries of the same protein (UniProt P11362 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5EW8 1.63 Å, Fibroblast growth factor receptor 1 in complex with jnj-4275693
4WUN 1.65 Å, Structure of FGFR1 in complex with AZD4547 (N-{3-[2-(3,5-DIMETHOXYPHENYL)ETHYL]-1H-PYRAZO…
9U7G 1.66 Å, FGFR1 kinase domain with a macrocyclic compound 8g
7OZB 1.71 Å, FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 38.
8XZ7 1.75 Å, FGFR1 kinase domain with a covalent inhibitor 10h
9UHI 1.76 Å, FGFR1 kinase domain with a covalent inhibitor 9o
9VLJ 1.81 Å, Crystal structure of FGFR1 in complex with covalent inhibitor 10a
7OZD 1.82 Å, FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 34.
7OZF 1.82 Å, FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 19.
9UHC 1.88 Å, FGFR1 kinase domain with a covalent inhibitor 9p
9WFK 1.89 Å, Crystal structure of FGFR1 kinase domain in complex with…
9WGT 1.9 Å, Crystal structure of FGFR1 kinase domain in complex with…

Browse structure collections

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