Magnesium in PDB 6rsw: Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin

The structure of Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin, PDB code: 6rsw was solved by T.Kotila, K.Kogan, P.Lappalainen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.45 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	87.370, 54.490, 87.830, 90.00, 93.61, 90.00
R / Rfree (%)	16.6 / 19.4

The binding sites of Magnesium atom in the Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin (pdb code 6rsw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin, PDB code: 6rsw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:31.6 occ:1.00 O3B A:ADP402 2.0 26.3 1.0 O A:HOH532 2.0 26.6 1.0 O A:HOH530 2.1 29.9 1.0 O A:HOH575 2.1 28.6 1.0 O A:HOH555 2.1 30.4 1.0 O A:HOH605 2.2 29.1 1.0 PB A:ADP402 3.3 28.1 1.0 O2B A:ADP402 3.6 25.3 1.0 O2A A:ADP402 4.0 27.8 1.0 NZ A:LYS18 4.1 24.6 1.0 O3A A:ADP402 4.1 26.0 1.0 O A:HOH569 4.2 35.6 1.0 CA A:GLY13 4.2 27.1 1.0 OD1 A:ASP154 4.2 31.9 1.0 OE1 A:GLN137 4.3 30.5 1.0 OD2 A:ASP11 4.4 34.4 1.0 O1B A:ADP402 4.4 29.9 1.0 OD2 A:ASP154 4.4 41.3 1.0 OD1 A:ASP11 4.4 33.7 1.0 O A:HOH617 4.4 31.6 1.0 O A:HOH665 4.5 32.0 1.0 PA A:ADP402 4.6 28.7 1.0 CD A:GLN137 4.6 41.0 1.0 CG A:ASP154 4.7 33.1 1.0 CG A:ASP11 4.8 33.7 1.0 CE A:LYS18 4.9 30.5 1.0 O A:HOH503 4.9 47.7 1.0 O1A A:ADP402 4.9 29.1 1.0 N A:SER14 5.0 27.0 1.0

Magnesium binding site 2 out of 2 in the Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hfd Domain of Mouse CAP1 Bound to the Pointed End of G-Actin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:34.9 occ:1.00 O B:GLU296 2.6 33.7 1.0 O A:HOH699 2.7 37.9 1.0 O B:HOH580 2.7 42.9 1.0 O A:HOH658 2.8 32.6 1.0 O B:HOH578 2.8 46.4 1.0 O A:HOH564 2.9 35.9 1.0 C B:GLU296 3.7 32.8 1.0 ND2 A:ASN296 4.0 25.8 1.0 O B:HOH539 4.1 47.7 1.0 CA B:ILE297 4.2 31.0 1.0 O A:HOH692 4.2 46.2 1.0 OD1 A:ASN296 4.3 31.5 1.0 O B:HOH617 4.3 33.0 1.0 N B:ILE297 4.4 31.0 1.0 O B:HOH567 4.5 30.0 1.0 CG A:ASN296 4.6 28.4 1.0 O A:HOH540 4.7 49.1 1.0 O A:HOH829 4.7 38.8 1.0 OE2 B:GLU302 4.7 73.3 1.0 CA B:GLU296 4.7 28.6 1.0 CB B:GLU296 4.8 29.6 1.0 O B:HOH504 4.9 29.4 1.0 NZ A:LYS326 4.9 79.6 1.0 C B:ILE297 4.9 36.0 1.0

T.Kotila, H.Wioland, G.Enkavi, K.Kogan, I.Vattulainen, A.Jegou, G.Romet-Lemonne, P.Lappalainen. Mechanism of Synergistic Actin Filament Pointed End Depolymerization By Cyclase-Associated Protein and Cofilin. Nat Commun V. 10 5320 2019.
ISSN: ESSN 2041-1723
PubMed: 31757941
DOI: 10.1038/S41467-019-13213-2