Magnesium in PDB 4yc7: Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp

The structure of Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp, PDB code: 4yc7 was solved by S.Kuhn, M.Geyer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.40 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.094, 91.094, 144.275, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 25.3

The binding sites of Magnesium atom in the Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp (pdb code 4yc7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp, PDB code: 4yc7:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Human FMNL2 Gbd-FH3 Domains Bound to CDC42-Gppnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:55.8 occ:1.00 O2B A:GNP201 2.7 32.6 1.0 O2G A:GNP201 2.8 38.8 1.0 OG1 A:THR16 2.8 46.0 1.0 O A:HOH315 2.8 32.8 1.0 O2A A:GNP201 2.9 45.9 1.0 O A:VAL32 2.9 59.3 1.0 OG1 A:THR34 3.1 54.5 1.0 CB A:THR16 3.3 44.2 1.0 PB A:GNP201 3.6 42.5 1.0 PA A:GNP201 3.7 48.5 1.0 O A:HOH316 3.7 51.7 1.0 C A:VAL32 3.8 66.2 1.0 N A:THR34 3.8 47.5 1.0 PG A:GNP201 3.8 47.3 1.0 O3A A:GNP201 3.9 51.0 1.0 N3B A:GNP201 3.9 49.3 1.0 CG2 A:THR16 4.0 42.1 1.0 CA A:PRO33 4.0 69.7 1.0 CE2 A:TYR31 4.1 93.8 1.0 O1A A:GNP201 4.1 39.7 1.0 C A:PRO33 4.2 58.6 1.0 N A:PRO33 4.3 71.4 1.0 CB A:THR34 4.3 48.8 1.0 O3G A:GNP201 4.3 49.9 1.0 CD2 A:TYR31 4.4 93.2 1.0 O A:HOH322 4.5 57.6 1.0 CA A:THR34 4.6 53.9 1.0 CA A:THR16 4.6 48.2 1.0 N A:VAL32 4.7 77.6 1.0 N A:THR16 4.7 45.5 1.0 CA A:VAL32 4.8 68.9 1.0 O1B A:GNP201 4.9 44.8 1.0

S.Kuhn, C.Erdmann, F.Kage, J.Block, L.Schwenkmezger, A.Steffen, K.Rottner, M.Geyer. The Structure of FMNL2-CDC42 Yields Insights Into the Mechanism of Lamellipodia and Filopodia Formation. Nat Commun V. 6 7088 2015.
ISSN: ESSN 2041-1723
PubMed: 25963737
DOI: 10.1038/NCOMMS8088