Calcium in PDB 1y64: BNI1P Formin Homology 2 Domain Complexed with Atp-Actin

The structure of BNI1P Formin Homology 2 Domain Complexed with Atp-Actin, PDB code: 1y64 was solved by T.Otomo, D.R.Tomchick, C.Otomo, S.C.Panchal, M.Machius, M.K.Rosen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 3.05
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	231.997, 56.229, 100.945, 90.00, 107.70, 90.00
R / Rfree (%)	28.9 / 31.3

The binding sites of Calcium atom in the BNI1P Formin Homology 2 Domain Complexed with Atp-Actin (pdb code 1y64). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the BNI1P Formin Homology 2 Domain Complexed with Atp-Actin, PDB code: 1y64:

Calcium binding site 1 out of 1 in the BNI1P Formin Homology 2 Domain Complexed with Atp-Actin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of BNI1P Formin Homology 2 Domain Complexed with Atp-Actin within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca382 b:97.1 occ:1.00 O3B A:ATP2000 2.7 97.1 1.0 NE2 A:GLN137 2.9 98.3 1.0 O1B A:ATP2000 3.2 97.1 1.0 O1G A:ATP2000 3.5 97.1 1.0 PG A:ATP2000 3.5 97.1 1.0 CD A:GLN137 3.5 98.3 1.0 OE1 A:GLN137 3.5 98.3 1.0 PB A:ATP2000 3.6 97.1 1.0 OD2 A:ASP11 3.7 61.1 1.0 O2G A:ATP2000 3.8 97.1 1.0 OD1 A:ASP154 3.9 63.9 1.0 NZ A:LYS18 3.9 53.8 1.0 O1A A:ATP2000 4.3 97.1 1.0 OD2 A:ASP154 4.4 63.9 1.0 CG A:ASP154 4.5 63.9 1.0 O3A A:ATP2000 4.6 97.1 1.0 CG1 A:VAL339 4.6 89.0 1.0 CA A:GLY13 4.6 40.6 1.0 O2B A:ATP2000 4.7 97.1 1.0 CG A:ASP11 4.7 61.1 1.0 CG A:GLN137 4.8 98.3 1.0 O A:ASN12 4.9 79.0 1.0 OD1 A:ASP11 4.9 61.1 1.0 O3G A:ATP2000 4.9 97.1 1.0 PA A:ATP2000 5.0 97.1 1.0

T.Otomo, D.R.Tomchick, C.Otomo, S.C.Panchal, M.Machius, M.K.Rosen. Structural Basis of Actin Filament Nucleation and Processive Capping By A Formin Homology 2 Domain Nature V. 433 488 2005.
ISSN: ISSN 0028-0836
PubMed: 15635372
DOI: 10.1038/NATURE03251