Magnesium in PDB 6fm2: Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin

The structure of Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin, PDB code: 6fm2 was solved by T.M.Kotila, K.Kogan, P.Lappalainen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.57 / 2.80
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	73.833, 73.833, 453.377, 90.00, 90.00, 120.00
R / Rfree (%)	18.3 / 23.4

The binding sites of Magnesium atom in the Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin (pdb code 6fm2). 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 Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin, PDB code: 6fm2:

Magnesium binding site 1 out of 1 in the Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Carp Domain of Mouse Cyclase-Associated Protein 1 (CAP1) Bound to Adp- Actin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:79.1 occ:1.00 O A:HOH506 1.9 78.0 1.0 O A:HOH504 2.1 70.2 1.0 O A:HOH528 2.2 88.4 1.0 O A:HOH527 2.3 82.9 1.0 O2B A:ADP402 2.6 0.9 1.0 O A:HOH534 3.5 87.2 1.0 PB A:ADP402 3.8 0.7 1.0 OD1 A:ASP154 3.8 0.4 1.0 O3B A:ADP402 3.9 0.0 1.0 OE1 A:GLN137 3.9 0.7 1.0 CD A:GLN137 4.3 0.5 1.0 OD1 A:ASP11 4.3 0.9 1.0 CG A:GLN137 4.4 0.8 1.0 OD2 A:ASP11 4.5 0.8 1.0 OD2 A:ASP154 4.5 0.3 1.0 CG A:ASP154 4.5 1.0 1.0 O A:HOH521 4.6 0.7 1.0 O2A A:ADP402 4.6 0.6 1.0 O3A A:ADP402 4.7 0.7 1.0 CA A:GLY13 4.7 98.6 1.0 O A:HOH503 4.7 0.0 1.0 CG2 A:VAL339 4.8 0.7 1.0 CG A:ASP11 4.9 0.7 1.0 O A:HOH545 4.9 90.8 1.0 O1B A:ADP402 4.9 0.8 1.0 NZ A:LYS18 5.0 0.8 1.0

T.Kotila, K.Kogan, G.Enkavi, S.Guo, I.Vattulainen, B.L.Goode, P.Lappalainen. Structural Basis of Actin Monomer Re-Charging By Cyclase-Associated Protein. Nat Commun V. 9 1892 2018.
ISSN: ESSN 2041-1723
PubMed: 29760438
DOI: 10.1038/S41467-018-04231-7