5HHC: Vascular endothelial growth factor A

Crystal Structure of Chemically Synthesized Heterochiral {RFX037 plus VEGF-A} Protein Complex in space group P21/n. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Mar 2016.

Method
X-ray diffraction
Resolution
2.1 Å
Organisms
Homo sapiens, synthetic construct
Chains
4
Atoms
2,877
Mol. weight
39.7 kDa
Released
9 Mar 2016

Explore 5HHC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5HHC contains 11 α-helices and 24 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.

Chains A and B: 4 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix71
β-strand811
α-helix91
α-helix10-178
β-strand1812
β-strand20-2783
α-helix28-314
β-strand39-4134
β-strand44-5183
β-strand5312
β-strand59-77194
β-strand81-99194
Chain C: 1 helix, 4 β-strands
ElementResiduesLengthSheet
β-strand8-1581
β-strand20-2781
α-helix30-4213
β-strand47-5481
β-strand59-6461
Chain D: 2 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand8-1584
β-strand20-2784
α-helix30-4415
β-strand47-5484
α-helix55-573
β-strand59-6464

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular endothelial growth factor AA, Bprotein102Homo sapiensP15692 (AlphaFold model)
D- Vascular endothelial growth factor-AC, Dprotein69synthetic construct
Sequence of entity 1 (A, B), FASTA
>5HHC_1 Vascular endothelial growth factor A (chains A, B)
GQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLE
CVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKD
Sequence of entity 2 (C, D), FASTA
>5HHC_2 D- Vascular endothelial growth factor-A (chains C, D)
RRRRRGGSTYKLILNGKTLKGETTTEAVDVFDAFDVFFVYAASNFSDFDDWTYDDATKTF
TVTEGGSDK

Primary citation

A Potent d-Protein Antagonist of VEGF-A is Nonimmunogenic, Metabolically Stable, and Longer-Circulating in Vivo. Uppalapati, M., Lee, D.J., Mandal, K. et al. ACS Chem Biol (2016) 11:1058-1065. DOI 10.1021/acschembio.5b01006 · PubMed

Other PDB entries of the same protein (UniProt P15692 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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