9U7E: Fibroblast growth factor receptor 2

FGFR2 kinase domain with a macrocyclic compound 8g. Determined by X-ray diffraction at 2.2 Å resolution. Released 21 Jan 2026.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,653
Mol. weight: 70.96 kDa
Ligands: A1EOH
Released: 21 Jan 2026

Explore 9U7E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9U7E contains 36 α-helices and 28 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: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	475	1	1
α-helix	478-480	3
β-strand	481-490	10	1
β-strand	493-501	9	1
β-strand	511-518	8	1
β-strand	524	1	2
α-helix	525-541	17
β-strand	547	1	3
α-helix	548-549	2
β-strand	550-554	5	1
β-strand	561-565	5	1
β-strand	570-571	2	3
α-helix	572-577	6
α-helix	597-599	3
α-helix	600-619	20
β-strand	622-623	2	4
α-helix	629-631	3
β-strand	632-634	3	3
β-strand	640-642	3	3
α-helix	645-647	3
β-strand	649-650	2	4
β-strand	666	1	5
α-helix	667-669	3
α-helix	672-676	5
α-helix	682-697	16
α-helix	701-702	2
α-helix	709-717	9
α-helix	722-725	4
α-helix	730-739	10
α-helix	744-746	3
α-helix	748-749	2
α-helix	750-761	12

Chain B: 18 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	468-470	3
β-strand	475	1	6
α-helix	478-480	3
β-strand	481-489	9	6
β-strand	494-501	8	6
β-strand	511-518	8	6
β-strand	524	1	5
α-helix	525-541	17
β-strand	547	1	7
α-helix	548-549	2
β-strand	550-554	5	6
β-strand	561-564	4	6
β-strand	570-571	2	7
α-helix	572-577	6
α-helix	600-619	20
β-strand	622-623	2	8
α-helix	629-631	3
β-strand	632-634	3	7
β-strand	640-642	3	7
α-helix	645-647	3
β-strand	649-650	2	8
β-strand	666	1	2
α-helix	667-669	3
α-helix	672-677	6
α-helix	682-697	16
α-helix	701-702	2
α-helix	709-717	9
α-helix	722-725	4
α-helix	730-739	10
α-helix	744-746	3
α-helix	748-749	2
α-helix	750-761	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fibroblast growth factor receptor 2	A, B	protein	304	Homo sapiens	P21802 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9U7E_1 Fibroblast growth factor receptor 2 (chains A, B)
EYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDAT
EKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGM
EYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIAD
FGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPY
PGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLT
TNEE

Ligands and cofactors

ID	Name	Formula	Copies
A1EOH	(E)-4-methyl-17-(1-methyl-1H-pyrazol-4-yl)-7,10-dioxa-4-aza-1(3,6)-imidazo[1,2-…	C21 H21 N7 O3	2

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

Primary citation

Design, Synthesis, and Biological Evaluation of the First Novel Macrocycle-Based FGFR Inhibitors That Overcome Clinically Acquired Resistance. Xiang, S., Chen, X., Lin, J. et al. J Med Chem (2026) 69:1178-1198. DOI 10.1021/acs.jmedchem.5c02462 · PubMed

Other PDB entries of the same protein (UniProt P21802 (AlphaFold model), which also has an AlphaFold model), best resolution first:

10OU 1.77 Å, FGFR2 mutant D650V with compound 12
2PVF 1.8 Å, Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase…
3B2T 1.8 Å, Structure of phosphotransferase
4J99 1.85 Å, Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Gain-of-Function…
10OO 1.85 Å, FGFR2 mutant D650V with compound 4 (AZD3463)
5UGL 1.86 Å, Crystal Structure of FGF Receptor 2 Tyrosine Kinase Domain Harboring the D650V…
3CAF 1.96 Å, Crystal Structure of hFGFR2 D2 Domain
10OQ 1.98 Å, FGFR2 mutant D650V with compound 6
9U7S 1.99 Å, FGFR2 kinase domain with a macrocyclic compound 8r
3CLY 2.0 Å, Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domains Trapped in…
8W3D 2.04 Å, TAS-120 covalent structure with FGFR2 molecular brake mutant
5UI0 2.05 Å, Crystal Structure of the Tyrosine Kinase Domain of FGF Receptor 2 harboring an…

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