1YWN: Vegfr2

Vegfr2 in complex with a novel 4-amino-furo[2,3-d]pyrimidine. Determined by X-ray diffraction at 1.71 Å resolution. Released 23 Aug 2005.

Method
X-ray diffraction
Resolution
1.71 Å
Organism
Homo sapiens
Chains
1
Atoms
2,512
Mol. weight
36.89 kDa
Ligands
LIF
Released
23 Aug 2005

Explore 1YWN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1YWN contains 18 α-helices and 12 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: 18 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix822-8254
β-strand82611
α-helix829-8313
β-strand832-84091
β-strand845-85281
β-strand860-86781
α-helix874-89017
β-strand89612
β-strand899-90351
β-strand911-91551
β-strand92112
α-helix922-9287
α-helix930-9323
β-strand93313
β-strand99813
α-helix1000-101920
α-helix1029-10313
β-strand1032-103432
α-helix1036-10383
β-strand1040-104232
α-helix1066-10694
α-helix1072-10776
α-helix1082-109716
α-helix1101-11022
α-helix1111-11199
α-helix1123-11264
α-helix1131-114010
α-helix1145-11473
α-helix1149-11502
α-helix1151-116515

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular endothelial growth factor receptor 2Aprotein316Homo sapiensP35968 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1YWN_1 Vascular endothelial growth factor receptor 2 (chains A)
MDPDELPLDEHCERLPYDASKWEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATCRTV
AVKMLKEGATHSEHRALMSELKILIHIGHHLNVVNLLGACTKPGGPLMVIVEFCKFGNLS
TYLRSKRNEFVPYKVAPEDLYKDFLTLEHLICYSFQVAKGMEFLASRKCIHRDLAARNIL
LSEKNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLL
WEIFSLGASPYPGVKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSE
LVEHLGNLLQANAQQD

Ligands and cofactors

IDNameFormulaCopies
LIFN-{4-[4-amino-6-(4-METHOXYPHENYL)FURO[2,3-d]pyrimidin-5-yl]phenyl}-N'-[2-fluoro…C27 H19 F4 N5 O31

Primary citation

Novel 4-amino-furo[2,3-d]pyrimidines as Tie-2 and VEGFR2 dual inhibitors. Miyazaki, Y., Matsunaga, S., Tang, J. et al. Bioorg Med Chem Lett (2005) 15:2203-2207. DOI 10.1016/j.bmcl.2005.03.034 · PubMed

Other PDB entries of the same protein (UniProt P35968 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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