4B6D: Atypical C1 domain of MgcRacGAP

Structure of the atypical C1 domain of MgcRacGAP. Determined by X-ray diffraction at 2.2 Å resolution. Released 12 Dec 2012.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
HOMO SAPIENS
Chains
6
Atoms
2,932
Mol. weight
41.82 kDa
Ligands
ZN
Released
12 Dec 2012

Explore 4B6D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 2 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand281-28221
β-strand28412
α-helix285-2873
β-strand289-29353
β-strand298-29924
β-strand306-30724
β-strand312-31653
β-strand322-32323
α-helix325-3306
Chains B, C and D: 2 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix285-2873
β-strand289-29355
β-strand298-29926
β-strand306-30726
β-strand312-31655
β-strand322-32325
α-helix325-3306
Chain E: 2 helices, 6 β-strands
ElementResiduesLengthSheet
α-helix285-2873
β-strand289-293511
β-strand298-299212
β-strand306-307212
β-strand312-316511
β-strand322-323211
α-helix325-3306
β-strand33312
Chain F: 2 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand284-28521
α-helix286-2872
β-strand289-293513
β-strand298-299214
β-strand306-307214
β-strand312-316513
β-strand322-323213
α-helix325-3306

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Rac gtpase-activating protein 1A, B, C, D, E, Fprotein61HOMO SAPIENSQ9H0H5 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>4B6D_1 RAC GTPASE-ACTIVATING PROTEIN 1 (chains A, B, C, D, E, F)
GPLGSMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPT
L

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn12

Water and common crystallization additives (GOL) are not listed.

Primary citation

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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