Crystal structure of MDIA1-TSH GBD-FH3 in complex with CDC42-GMPPNP. Determined by X-ray diffraction at 2.7 Å resolution. Released 14 Oct 2008.
Explore 3EG5 in 3D Show helices and sheets RCSB PDB PDBe
3EG5 contains 60 α-helices and 16 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 | 4-9 | 6 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 1 |
| β-strand | 49-58 | 10 | 1 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 1 |
| α-helix | 117-119 | 3 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 154-156 | 3 | 1 |
| α-helix | 165-177 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 85-93 | 9 | |
| α-helix | 98-105 | 8 | |
| α-helix | 109-122 | 14 | |
| α-helix | 136-143 | 8 | |
| α-helix | 149-165 | 17 | |
| α-helix | 168-190 | 23 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-226 | 8 | |
| α-helix | 231-237 | 7 | |
| α-helix | 244-258 | 15 | |
| α-helix | 266-281 | 16 | |
| α-helix | 287-291 | 5 | |
| β-strand | 295 | 1 | 2 |
| β-strand | 297 | 1 | 2 |
| α-helix | 299-313 | 15 | |
| α-helix | 319-331 | 13 | |
| α-helix | 334-341 | 8 | |
| α-helix | 347-377 | 31 | |
| α-helix | 381-391 | 11 | |
| α-helix | 398-407 | 10 | |
| α-helix | 418-433 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 3 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 3 |
| β-strand | 49-58 | 10 | 3 |
| α-helix | 62-64 | 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 | 117-121 | 5 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 154-156 | 3 | 3 |
| α-helix | 165-177 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cell division control protein 42 homolog | A, C | protein | 178 | Mus musculus | P60766 (AlphaFold model) |
| Protein diaphanous homolog 1 | B, D | protein | 383 | Mus musculus | O08808 (AlphaFold model) |
>3EG5_1 Cell division control protein 42 homolog (chains A, C) MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQRGLKNVFDEAILAALE
>3EG5_2 Protein diaphanous homolog 1 (chains B, D) DPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMN QKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLTSHPVSWVQTFGAEGLASLLDILKR LHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMI DAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQL INALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLK GRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEEC VSQIVLHKNGTDPDFKCRHLQID
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 2 |
| MG | Magnesium ion | Mg | 2 |
Specificity of Interactions between mDia Isoforms and Rho Proteins. Lammers, M., Meyer, S., Kuhlmann, D. et al. J Biol Chem (2008) 283:35236-35246. DOI 10.1074/jbc.M805634200 · PubMed
Other PDB entries of the same protein (UniProt P60766 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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