Complex structure of human IGF2R domains 11-13 bound to igf-II. Determined by X-ray diffraction at 4.1 Å resolution. Released 11 Dec 2007.
Explore 2V5P in 3D Show helices and sheets RCSB PDB PDBe
2V5P contains 42 α-helices and 111 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1517-1519 | 3 | 1 |
| β-strand | 1526-1528 | 3 | 1 |
| α-helix | 1530-1532 | 3 | |
| β-strand | 1538-1542 | 5 | 2 |
| β-strand | 1546-1550 | 5 | 2 |
| α-helix | 1560 | 1 | |
| β-strand | 1563 | 1 | 3 |
| β-strand | 1565 | 1 | 2 |
| β-strand | 1576 | 1 | 3 |
| β-strand | 1581-1584 | 4 | 2 |
| β-strand | 1587-1592 | 6 | 2 |
| β-strand | 1593 | 1 | 3 |
| β-strand | 1597 | 1 | 4 |
| α-helix | 1598 | 1 | |
| β-strand | 1605 | 1 | 4 |
| β-strand | 1607-1614 | 8 | 2 |
| β-strand | 1625-1630 | 6 | 2 |
| β-strand | 1635-1642 | 8 | 2 |
| α-helix | 1643-1645 | 3 | |
| β-strand | 1653-1656 | 4 | 5 |
| β-strand | 1659-1662 | 4 | 5 |
| α-helix | 1664-1666 | 3 | |
| β-strand | 1673-1674 | 2 | 6 |
| α-helix | 1675-1676 | 2 | |
| β-strand | 1690-1692 | 3 | 6 |
| α-helix | 1697-1700 | 4 | |
| β-strand | 1712-1714 | 3 | 6 |
| β-strand | 1722-1725 | 4 | 6 |
| β-strand | 1726-1727 | 2 | 7 |
| α-helix | 1731 | 1 | |
| β-strand | 1732-1733 | 2 | 7 |
| β-strand | 1740-1745 | 6 | 7 |
| β-strand | 1760-1766 | 7 | 7 |
| β-strand | 1776-1779 | 4 | 7 |
| β-strand | 1786-1791 | 6 | 7 |
| α-helix | 1792-1794 | 3 | |
| α-helix | 1798-1800 | 3 | |
| β-strand | 1805-1807 | 3 | 8 |
| β-strand | 1814-1816 | 3 | 8 |
| α-helix | 1817-1819 | 3 | |
| β-strand | 1825 | 1 | 9 |
| β-strand | 1828-1829 | 2 | 10 |
| β-strand | 1832-1833 | 2 | 10 |
| β-strand | 1834-1836 | 3 | 9 |
| β-strand | 1853 | 1 | 11 |
| β-strand | 1855-1857 | 3 | 9 |
| β-strand | 1864-1865 | 2 | 9 |
| β-strand | 1868-1877 | 10 | 11 |
| β-strand | 1882-1888 | 7 | 11 |
| β-strand | 1892 | 1 | 12 |
| α-helix | 1893-1895 | 3 | |
| β-strand | 1896-1897 | 2 | 13 |
| α-helix | 1901 | 1 | |
| β-strand | 1902 | 1 | 13 |
| α-helix | 1903 | 1 | |
| β-strand | 1907-1909 | 3 | 14 |
| β-strand | 1912-1914 | 3 | 14 |
| β-strand | 1918 | 1 | 15 |
| β-strand | 1926-1928 | 3 | 15 |
| β-strand | 1932 | 1 | 14 |
| α-helix | 1933-1936 | 4 | |
| β-strand | 1939-1941 | 3 | 15 |
| β-strand | 1942-1943 | 2 | 13 |
| β-strand | 1948 | 1 | 12 |
| β-strand | 1950-1957 | 8 | 11 |
| β-strand | 1966-1972 | 7 | 11 |
| β-strand | 1976-1983 | 8 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1517-1519 | 3 | 16 |
| α-helix | 1525 | 1 | |
| β-strand | 1526-1528 | 3 | 16 |
| α-helix | 1530-1532 | 3 | |
| β-strand | 1538-1542 | 5 | 17 |
| β-strand | 1546-1550 | 5 | 17 |
| α-helix | 1560 | 1 | |
| β-strand | 1563 | 1 | 18 |
| β-strand | 1565 | 1 | 17 |
| β-strand | 1576 | 1 | 18 |
| β-strand | 1581-1583 | 3 | 19 |
| β-strand | 1588-1592 | 5 | 19 |
| β-strand | 1593 | 1 | 18 |
| β-strand | 1597 | 1 | 20 |
| α-helix | 1604 | 1 | |
| β-strand | 1605 | 1 | 20 |
| α-helix | 1606 | 1 | |
| β-strand | 1607-1614 | 8 | 19 |
| β-strand | 1625-1630 | 6 | 19 |
| β-strand | 1635-1642 | 8 | 19 |
| α-helix | 1643-1645 | 3 | |
| β-strand | 1653-1656 | 4 | 21 |
| β-strand | 1659-1662 | 4 | 21 |
| α-helix | 1664-1666 | 3 | |
| β-strand | 1673-1674 | 2 | 22 |
| α-helix | 1675-1676 | 2 | |
| β-strand | 1690-1692 | 3 | 22 |
| α-helix | 1697-1699 | 3 | |
| β-strand | 1712-1714 | 3 | 22 |
| α-helix | 1720-1721 | 2 | |
| β-strand | 1722-1725 | 4 | 22 |
| β-strand | 1726-1727 | 2 | 23 |
| α-helix | 1731 | 1 | |
| β-strand | 1732-1733 | 2 | 23 |
| β-strand | 1740-1745 | 6 | 23 |
| β-strand | 1759-1766 | 8 | 23 |
| β-strand | 1776-1779 | 4 | 23 |
| β-strand | 1784-1791 | 8 | 23 |
| α-helix | 1792-1794 | 3 | |
| α-helix | 1796-1800 | 5 | |
| β-strand | 1805-1807 | 3 | 24 |
| β-strand | 1814-1816 | 3 | 24 |
| β-strand | 1828-1829 | 2 | 25 |
| β-strand | 1832-1833 | 2 | 25 |
| β-strand | 1836 | 1 | 26 |
| β-strand | 1853 | 1 | 27 |
| β-strand | 1855 | 1 | 26 |
| β-strand | 1856-1857 | 2 | 28 |
| β-strand | 1858 | 1 | 25 |
| β-strand | 1864-1865 | 2 | 28 |
| β-strand | 1868-1877 | 10 | 27 |
| β-strand | 1882-1888 | 7 | 27 |
| β-strand | 1892 | 1 | 29 |
| α-helix | 1893-1895 | 3 | |
| β-strand | 1896-1897 | 2 | 30 |
| α-helix | 1901 | 1 | |
| β-strand | 1902 | 1 | 30 |
| α-helix | 1903 | 1 | |
| β-strand | 1907-1909 | 3 | 31 |
| β-strand | 1912-1914 | 3 | 31 |
| β-strand | 1918 | 1 | 32 |
| β-strand | 1926-1928 | 3 | 32 |
| β-strand | 1932 | 1 | 31 |
| α-helix | 1933-1936 | 4 | |
| β-strand | 1939-1941 | 3 | 32 |
| β-strand | 1942-1943 | 2 | 30 |
| β-strand | 1948 | 1 | 29 |
| β-strand | 1950-1955 | 6 | 27 |
| β-strand | 1956-1957 | 2 | 33 |
| β-strand | 1966-1973 | 8 | 27 |
| β-strand | 1976-1981 | 6 | 27 |
| β-strand | 1982-1983 | 2 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-20 | 10 | |
| β-strand | 26 | 1 | 34 |
| α-helix | 42-46 | 5 | |
| α-helix | 54-57 | 4 | |
| β-strand | 60 | 1 | 34 |
| α-helix | 61-62 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-20 | 10 | |
| α-helix | 22-24 | 3 | |
| β-strand | 26 | 1 | 35 |
| α-helix | 42 | 1 | |
| α-helix | 43-47 | 5 | |
| α-helix | 54-57 | 4 | |
| β-strand | 60 | 1 | 35 |
| α-helix | 61-62 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cation-independent mannose-6-phosphate receptor | A, B | protein | 492 | Homo sapiens | P11717 (AlphaFold model) |
| Insulin-like growth factor II | C, D | protein | 67 | Homo sapiens | P01344 (AlphaFold model) |
>2V5P_1 CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR (chains A, B) MKSNEHDDCQVTNPSTGHLFDLSSLSGRAGFTAAYSEKGLVYMSICGENENCPPGVGACF GQTRISVGKANKRLRYVDQVLQLVYKDGSPCPSKSGLSYKSVISFVCRPEAGPTNRPMLI SLDKQTCTLFFSWHTPLACEQATECSVRNGSSIVDLSPLIHRTGGYEAYDESEDDASDTN PDFYINICQPLNPMHAVPCPAGAAVCKVPIDGPPIDIGRVAGPPILNPIANEIYLNFESS TPCLADKHFNYTSLIAFHCKRGVSMGTPKLLRTSECDFVFEWETPVVCPDEVRMDGCTLT DEQLLYSFNLSSLSTSTFKVTRDSRTYSVGVCTFAVGPEQGGCKDGGVCLLSGTKGASFG RLQSMKLDYRHQDEAVVLSYVNGDRCPPETDDGVPCVFPFIFNGKSYEECIIESRAKLWC STTADYDRDHEWGFCRHSNSYRTSSIIFKCDEDEDIGRPQVFSEVRGCDVTFEWKTKVVC PPKKLKHHHHHH
>2V5P_2 INSULIN-LIKE GROWTH FACTOR II (chains C, D) AYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYC ATPAKSE
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
Structure and Functional Analysis of the Igf-II/Igf2R Interaction. Brown, J., Delaine, C., Zaccheo, O.J. et al. EMBO J (2008) 27:265. DOI 10.1038/SJ.EMBOJ.7601938 · PubMed
Other PDB entries of the same protein (UniProt P11717 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2V5P directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.