Crystal structure of vegf-C in complex with domains 2 and 3 of VEGFR2 in a tetragonal crystal form. Determined by X-ray diffraction at 3.1 Å resolution. Released 9 Feb 2010.
Explore 2X1X in 3D Show helices and sheets RCSB PDB PDBe
2X1X contains 8 α-helices and 24 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 114-128 | 15 | |
| β-strand | 132-139 | 8 | 1 |
| α-helix | 140 | 1 | |
| α-helix | 141-145 | 5 | |
| β-strand | 150-153 | 4 | 2 |
| β-strand | 156-163 | 8 | 1 |
| β-strand | 171-189 | 19 | 2 |
| β-strand | 197-213 | 17 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 125 | 1 | 3 |
| β-strand | 133-138 | 6 | 4 |
| α-helix | 139 | 1 | |
| α-helix | 141 | 1 | |
| β-strand | 145-148 | 4 | 5 |
| β-strand | 152 | 1 | 3 |
| β-strand | 159-164 | 6 | 4 |
| β-strand | 168-170 | 3 | 4 |
| β-strand | 178-180 | 3 | 5 |
| β-strand | 184-188 | 5 | 5 |
| α-helix | 189-191 | 3 | |
| β-strand | 197-202 | 6 | 4 |
| β-strand | 209-210 | 2 | 4 |
| β-strand | 213-218 | 6 | 4 |
| β-strand | 223-229 | 7 | 6 |
| β-strand | 234-237 | 4 | 7 |
| α-helix | 240-241 | 2 | |
| β-strand | 242-250 | 9 | 6 |
| β-strand | 257-261 | 5 | 7 |
| β-strand | 270-277 | 8 | 6 |
| β-strand | 286-294 | 9 | 6 |
| α-helix | 299-301 | 3 | |
| β-strand | 303-311 | 9 | 7 |
| β-strand | 314-325 | 12 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vascular endothelial growth factor C | E | protein | 110 | HOMO SAPIENS | P49767 (AlphaFold model) |
| Vascular endothelial growth factor receptor 2 | R | protein | 213 | HOMO SAPIENS | P35968 (AlphaFold model) |
>2X1X_1 VASCULAR ENDOTHELIAL GROWTH FACTOR C (chains E) AHYNTEILKSIDNEWRKTQCMPREVAIDVGKEFGVATNTFFKPPCVSVYRCGGCCNSEGL QCMNTSTSYLSKTLFEITVPLSQGPKPVTISFANHTSCRCMSKLHHHHHH
>2X1X_2 VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (chains R) DYRSPFIASVSDQHGVVYITENKNKTVVIPCLGSISNLNVSLCARYPEKRFVPDGNRISW DSKKGFTIPSYMISYAGMVFCEAKINDESYQSIMYIVVVVGYRIYDVVLSPSHGIELSVG EKLVLNCTARTELNVGIDFNWEYPSSKHQHKKLVNRDLKTQSGSEMKKFLSTLTIDGVTR SDQGLYTCAASSGLMTKKNSTFVRVHEDPIEGR
Structural Determinants of Growth Factor Binding and Specificity by Vegf Receptor 2. Leppanen, V.-M., Prota, A.E., Jeltsch, M. et al. Proc Natl Acad Sci U S A (2010) 107:2425. DOI 10.1073/PNAS.0914318107 · PubMed
Other PDB entries of the same protein (UniProt P49767 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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