2PVY: Fibroblast growth factor receptor 2

Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome. Determined by X-ray diffraction at 2.2 Å resolution. Released 25 Sept 2007.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
4
Atoms
9,429
Mol. weight
150.79 kDa
Ligands
ACP
Released
25 Sept 2007

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

Secondary structure: helices and β-sheets

2PVY contains 74 α-helices and 58 β-strands across 4 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, 16 β-strands

ElementResiduesLengthSheet
β-strand47511
α-helix478-4803
β-strand481-48661
β-strand495-50171
β-strand511-51771
β-strand52412
α-helix525-54117
β-strand54713
α-helix548-5492
β-strand550-55451
β-strand561-56551
β-strand57113
α-helix572-5787
α-helix580-5812
α-helix594-5963
α-helix600-61920
β-strand622-62324
α-helix629-6313
β-strand632-63543
β-strand639-64243
β-strand649-65024
β-strand657-65825
β-strand66616
α-helix667-6693
α-helix672-6776
β-strand679-68025
α-helix682-69716
α-helix701-7022
α-helix709-7179
α-helix722-7254
α-helix730-73910
α-helix744-7463
α-helix748-7492
α-helix750-76314
Chain B: 20 helices, 13 β-strands
ElementResiduesLengthSheet
α-helix468-4703
β-strand47517
α-helix478-4803
β-strand481-48667
β-strand495-50177
β-strand511-51777
β-strand52418
α-helix525-54117
β-strand54719
α-helix548-5492
β-strand550-55457
β-strand561-56557
β-strand57119
α-helix572-5787
α-helix580-5823
α-helix594-5963
α-helix597-5993
α-helix600-61920
β-strand622-623210
α-helix629-6313
β-strand632-63439
β-strand640-64239
β-strand649-650210
α-helix667-6693
α-helix672-6765
α-helix682-69716
α-helix701-7022
α-helix709-7179
α-helix722-7254
α-helix730-73910
α-helix744-7463
α-helix748-7492
α-helix750-76314
Chain C: 18 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix472-4743
β-strand475111
α-helix478-4803
β-strand481-486611
β-strand495-501711
β-strand511-517711
β-strand52416
α-helix525-53915
β-strand547112
β-strand550-554511
β-strand561-565511
β-strand571112
α-helix572-5787
α-helix580-5812
α-helix597-5993
α-helix600-61920
β-strand622-623213
α-helix629-6313
β-strand632-635412
β-strand639-642412
β-strand649-650213
β-strand66612
α-helix667-6693
α-helix672-6765
α-helix682-69716
α-helix701-7022
α-helix709-7179
α-helix722-7254
α-helix730-73910
α-helix744-7463
α-helix748-7492
α-helix750-76314
Chain D: 18 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand475114
α-helix478-4803
β-strand481-486614
β-strand495-501714
β-strand511-517714
α-helix525-54117
β-strand547115
α-helix548-5492
β-strand550-554514
β-strand561-565514
α-helix566-5672
β-strand571115
α-helix572-5776
α-helix580-5823
α-helix600-61920
β-strand622-623216
α-helix629-6313
β-strand632-635415
β-strand639-642415
β-strand649-650216
β-strand657-658217
β-strand66618
α-helix667-6693
α-helix672-6776
β-strand679-680217
α-helix682-69716
α-helix701-7022
α-helix709-7179
α-helix722-7254
α-helix730-73910
α-helix744-7463
α-helix748-7492
α-helix750-76213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fibroblast growth factor receptor 2A, B, C, Dprotein324Homo sapiensP21802 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>2PVY_1 Fibroblast growth factor receptor 2 (chains A, B, C, D)
MGSSHHHHHHSQDPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGAFGQVVMAEAVGID
KDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIV
EYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIH
RDLAARNVLVTENNVMKIADFGLARDINNIDYYKNTTNGRLPVKWMAPEALFDRVYTHQS
DVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVP
SQRPTFKQLVEDLDRILTLTTNEE

Ligands and cofactors

IDNameFormulaCopies
ACPPhosphomethylphosphonic acid adenylate esterC11 H18 N5 O12 P34

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

Primary citation

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases. Chen, H., Ma, J., Li, W. et al. Mol Cell (2007) 27:717-730. DOI 10.1016/j.molcel.2007.06.028 · PubMed

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

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