Structure of the atypical C1 domain of MgcRacGAP. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Dec 2012.
Explore 4B6D in 3D Show helices and sheets RCSB PDB PDBe
4B6D contains 12 α-helices and 34 β-strands across 6 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 | 281-282 | 2 | 1 |
| β-strand | 284 | 1 | 2 |
| α-helix | 285-287 | 3 | |
| β-strand | 289-293 | 5 | 3 |
| β-strand | 298-299 | 2 | 4 |
| β-strand | 306-307 | 2 | 4 |
| β-strand | 312-316 | 5 | 3 |
| β-strand | 322-323 | 2 | 3 |
| α-helix | 325-330 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 285-287 | 3 | |
| β-strand | 289-293 | 5 | 5 |
| β-strand | 298-299 | 2 | 6 |
| β-strand | 306-307 | 2 | 6 |
| β-strand | 312-316 | 5 | 5 |
| β-strand | 322-323 | 2 | 5 |
| α-helix | 325-330 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 285-287 | 3 | |
| β-strand | 289-293 | 5 | 11 |
| β-strand | 298-299 | 2 | 12 |
| β-strand | 306-307 | 2 | 12 |
| β-strand | 312-316 | 5 | 11 |
| β-strand | 322-323 | 2 | 11 |
| α-helix | 325-330 | 6 | |
| β-strand | 333 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 284-285 | 2 | 1 |
| α-helix | 286-287 | 2 | |
| β-strand | 289-293 | 5 | 13 |
| β-strand | 298-299 | 2 | 14 |
| β-strand | 306-307 | 2 | 14 |
| β-strand | 312-316 | 5 | 13 |
| β-strand | 322-323 | 2 | 13 |
| α-helix | 325-330 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rac gtpase-activating protein 1 | A, B, C, D, E, F | protein | 61 | HOMO SAPIENS | Q9H0H5 (AlphaFold model) |
>4B6D_1 RAC GTPASE-ACTIVATING PROTEIN 1 (chains A, B, C, D, E, F) GPLGSMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPT L
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 12 |
Water and common crystallization additives (GOL) are not listed.
Centralspindlin Links the Mitotic Spindle to the Plasma Membrane During Cytokinesis. Lekomtsev, S., Su, K., Pye, V.E. et al. Nature (2012) 492:276. DOI 10.1038/NATURE11773 · PubMed
Other PDB entries of the same protein (UniProt Q9H0H5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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