1QSV: Vascular endothelial growth factor receptor 1

The vegf-binding domain of flt-1, 20 NMR structures. Determined by solution NMR. Released 10 Nov 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
810
Mol. weight
11.54 kDa
Released
10 Nov 1999

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

Secondary structure: helices and β-sheets

1QSV contains 3 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: 3 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand13511
α-helix1431
β-strand144-14852
β-strand154-15633
β-strand16011
α-helix163-1653
β-strand168-17142
β-strand175-17622
β-strand184-18743
β-strand191-19443
α-helix199-2013
β-strand204-21072
β-strand215-224102
β-strand22614
β-strand22814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular endothelial growth factor receptor 1Aprotein101Homo sapiensP17948 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1QSV_1 VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1 (chains A)
SDTGRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDS
RKGFIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQTNTI

Primary citation

Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states. Starovasnik, M.A., Christinger, H.W., Wiesmann, C. et al. J Mol Biol (1999) 293:531-544. DOI 10.1006/jmbi.1999.3134 · PubMed

Other PDB entries of the same protein (UniProt P17948 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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