4CL7: VEGFR-1 domain 2 in presence of Cobalt

Crystal structure of VEGFR-1 domain 2 in presence of Cobalt. Determined by X-ray diffraction at 2.0 Å resolution. Released 28 Jan 2015.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
3,326
Mol. weight
43.83 kDa
Ligands
CO
Released
28 Jan 2015

Explore 4CL7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CL7 contains 10 α-helices and 41 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: 3 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand13511
α-helix1431
β-strand144-14852
β-strand154-15633
β-strand16011
β-strand167-17152
β-strand175-17732
α-helix178-1792
β-strand184-18743
β-strand191-19443
α-helix199-2013
β-strand204-21182
β-strand214-224112
Chain B: 2 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand13514
α-helix1431
β-strand144-14855
β-strand154-15636
β-strand16014
β-strand167-17155
β-strand175-17735
β-strand184-18746
β-strand191-19446
α-helix199-2013
β-strand203-21195
β-strand214-224115
Chain C: 2 helices, 11 β-strands
ElementResiduesLengthSheet
β-strand13517
α-helix1431
β-strand144-14858
β-strand154-15639
β-strand16017
β-strand167-17158
β-strand175-17738
β-strand18019
β-strand184-18749
β-strand191-19449
α-helix199-2013
β-strand203-21198
β-strand214-224118
Chain D: 3 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand135110
α-helix1431
β-strand144-148511
β-strand154-156312
β-strand160110
β-strand167-171511
β-strand175-177311
α-helix178-1792
β-strand184-187412
β-strand191-194412
α-helix199-2013
β-strand203-211911
β-strand214-2241111

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular endothelial growth factor receptor 1A, B, C, Dprotein94HOMO SAPIENSP17948 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4CL7_1 VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 1 (chains A, B, C, D)
GRPFVEMYSEIPEIIHMTEGRELVIPCRVTSPNITVTLKKFPLDTLIPDGKRIIWDSRKG
FIISNATYKEIGLLTCEATVNGHLYKTNYLTHRQ

Ligands and cofactors

IDNameFormulaCopies
COCobalt (II) ionCo5

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

Primary citation

Biophysical Studies of the Induced Dimerization of Human Vegf R Receptor 1 Binding Domain by Divalent Metals Competing with Vegf-A. Gaucher, J.-F., Reille-Seroussi, M., Gagey-Eilstein, N. et al. PLoS One (2016) 11:67755. DOI 10.1371/JOURNAL.PONE.0167755 · 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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