DbsCdc42(Y889F). Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Mar 2002.
Explore 1KZG in 3D Show helices and sheets RCSB PDB PDBe
1KZG contains 61 α-helices and 32 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 |
|---|---|---|---|
| α-helix | 625-654 | 30 | |
| α-helix | 655-659 | 5 | |
| α-helix | 660-662 | 3 | |
| α-helix | 665-667 | 3 | |
| α-helix | 673-676 | 4 | |
| α-helix | 679-683 | 5 | |
| α-helix | 686-691 | 6 | |
| α-helix | 692-697 | 6 | |
| α-helix | 698-702 | 5 | |
| α-helix | 708-710 | 3 | |
| α-helix | 711-717 | 7 | |
| α-helix | 721-723 | 3 | |
| α-helix | 724-742 | 19 | |
| α-helix | 746-755 | 10 | |
| α-helix | 761-772 | 12 | |
| α-helix | 775-784 | 10 | |
| α-helix | 792-815 | 24 | |
| β-strand | 818-819 | 2 | 1 |
| α-helix | 825-828 | 4 | |
| β-strand | 831-841 | 11 | 1 |
| β-strand | 859-866 | 8 | 1 |
| β-strand | 869-876 | 8 | 1 |
| β-strand | 888-896 | 9 | 1 |
| α-helix | 897-899 | 3 | |
| β-strand | 900-903 | 4 | 1 |
| β-strand | 906 | 1 | 2 |
| β-strand | 909 | 1 | 2 |
| β-strand | 912-917 | 6 | 1 |
| β-strand | 922-927 | 6 | 1 |
| α-helix | 931-960 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-10 | 8 | 3 |
| α-helix | 16-25 | 10 | |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 49-56 | 8 | 3 |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 3 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 3 |
| α-helix | 117-120 | 4 | |
| α-helix | 123-130 | 8 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-149 | 11 | |
| β-strand | 154-156 | 3 | 3 |
| α-helix | 165-176 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1625-1654 | 30 | |
| α-helix | 1655-1659 | 5 | |
| α-helix | 1660-1662 | 3 | |
| α-helix | 1673-1676 | 4 | |
| α-helix | 1679-1683 | 5 | |
| α-helix | 1686-1691 | 6 | |
| α-helix | 1692-1697 | 6 | |
| α-helix | 1698-1702 | 5 | |
| α-helix | 1708-1710 | 3 | |
| α-helix | 1711-1716 | 6 | |
| α-helix | 1721-1723 | 3 | |
| α-helix | 1724-1742 | 19 | |
| α-helix | 1746-1755 | 10 | |
| α-helix | 1761-1765 | 5 | |
| α-helix | 1767-1772 | 6 | |
| α-helix | 1775-1784 | 10 | |
| α-helix | 1792-1815 | 24 | |
| β-strand | 1818-1819 | 2 | 4 |
| α-helix | 1825-1828 | 4 | |
| β-strand | 1831-1841 | 11 | 4 |
| β-strand | 1859-1866 | 8 | 4 |
| β-strand | 1869-1874 | 6 | 4 |
| β-strand | 1889-1896 | 8 | 4 |
| α-helix | 1897-1899 | 3 | |
| β-strand | 1900-1903 | 4 | 4 |
| β-strand | 1906 | 1 | 5 |
| β-strand | 1909 | 1 | 5 |
| β-strand | 1912-1917 | 6 | 4 |
| α-helix | 1918-1920 | 3 | |
| β-strand | 1922-1927 | 6 | 4 |
| α-helix | 1931-1954 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1004-1010 | 7 | 6 |
| α-helix | 1016-1025 | 10 | |
| β-strand | 1040-1046 | 7 | 6 |
| β-strand | 1049-1056 | 8 | 6 |
| α-helix | 1068-1071 | 4 | |
| β-strand | 1077-1083 | 7 | 6 |
| α-helix | 1087-1092 | 6 | |
| α-helix | 1093-1097 | 5 | |
| α-helix | 1098-1104 | 7 | |
| β-strand | 1110-1115 | 6 | 6 |
| α-helix | 1117-1119 | 3 | |
| α-helix | 1123-1130 | 8 | |
| α-helix | 1136-1138 | 3 | |
| α-helix | 1139-1149 | 11 | |
| β-strand | 1153-1156 | 4 | 6 |
| α-helix | 1165-1176 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Guanine nucleotide exchange factor dbs | A, C | protein | 353 | Mus musculus | Q64096 (AlphaFold model) |
| CDC42 homolog | B, D | protein | 188 | Homo sapiens | P60953 (AlphaFold model) |
>1KZG_1 GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS (chains A, C) MGEEEESLAILRRHVMNELLDTERAYVEELLCVLEGYAAEMDNPLMAHLISTGLQNKKNI LFGNMEEIYHFHNRIFLRELESCIDCPELVGRCFLERMEEFQIYEKYCQNKPRSESLWRQ CSDCPFFQECQKKLDHKLSLDSYLLKPVQRITKYQLLLKEMLKYSKHCEGAEDLQEALSS ILGILKAVNDSMHLIAITGYDGNLGDLGKLLMQGSFSVWTDHKKGHTKVKELARFKPMQR HLFLHEKAVLFCKKREENGEGYEKAPSFSYKQSLNMTAVGITENVKGDTKKFEIWYNARE EVYIIQAPTPEIKAAWVNEIRKVLTSQLQACREASQHRALEQSHSLEHHHHHH
>1KZG_2 CDC42 HOMOLOG (chains B, D) MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP EPKKSRRS
A crystallographic view of interactions between Dbs and Cdc42: PH domain-assisted guanine nucleotide exchange. Rossman, K.L., Worthylake, D.K., Snyder, J.T. et al. EMBO J (2002) 21:1315-1326. DOI 10.1093/emboj/21.6.1315 · PubMed
Other PDB entries of the same protein (UniProt Q64096 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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