1MKK: Vascular Endothelial Growth Factor A

Disulfide deficient mutant of vascular endothelial growth factor A (C61A and C104A). Determined by X-ray diffraction at 1.32 Å resolution. Released 11 Dec 2002.

Method
X-ray diffraction
Resolution
1.32 Å
Organism
Homo sapiens
Chains
2
Atoms
1,733
Mol. weight
22.39 kDa
Released
11 Dec 2002

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

Secondary structure: helices and β-sheets

1MKK contains 6 α-helices and 12 β-strands across 2 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, 6 β-strands

ElementResiduesLengthSheet
β-strand1511
α-helix17-248
β-strand27-3482
α-helix35-384
α-helix40-423
β-strand46-4833
β-strand51-5882
β-strand67-83173
β-strand90-105163
Chain B: 3 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand14-1523
α-helix17-248
β-strand27-3484
α-helix35-384
β-strand46-4831
β-strand51-5884
β-strand67-83171
α-helix88-892
β-strand90-105161

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vascular Endothelial Growth Factor AA, Bprotein96Homo sapiensP15692 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1MKK_1 Vascular Endothelial Growth Factor A (chains A, B)
MVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCANDEGLECVPTE
ESNITMQIMRIKPHQGQHIGEMSFLQHNKCEARPKK

Primary citation

The cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factor. Muller, Y.A., Heiring, C., Misselwitz, R. et al. J Biol Chem (2002) 277:43410-43416. DOI 10.1074/jbc.M206438200 · PubMed

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

Browse structure collections

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