Calcium in PDB 2q31: Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48.

The structure of Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48., PDB code: 2q31 was solved by M.R.Sawaya, I.Pashkov, D.S.Kudryashov, E.Reisler, T.O.Yeates, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.07 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	108.253, 71.984, 54.703, 90.00, 104.68, 90.00
R / Rfree (%)	24.9 / 28.8

The binding sites of Calcium atom in the Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48. (pdb code 2q31). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48., PDB code: 2q31:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:27.0 occ:1.00 O2G A:ATP400 2.3 28.1 1.0 O1B A:ATP400 2.4 27.0 1.0 PG A:ATP400 3.6 28.1 1.0 OE1 A:GLN137 3.6 27.7 1.0 O A:HOH410 3.6 2.1 1.0 PB A:ATP400 3.7 26.5 1.0 O1A A:ATP400 3.7 29.0 1.0 O1G A:ATP400 4.0 27.8 1.0 CD A:GLN137 4.1 28.7 1.0 O3B A:ATP400 4.1 26.4 1.0 O3A A:ATP400 4.1 27.4 1.0 O A:HOH407 4.2 2.0 1.0 OD2 A:ASP11 4.2 29.7 1.0 NE2 A:GLN137 4.3 28.6 1.0 NZ A:LYS18 4.4 29.0 1.0 CA A:GLY13 4.4 27.9 1.0 PA A:ATP400 4.4 27.9 1.0 OD1 A:ASP11 4.4 31.0 1.0 CG2 A:VAL339 4.7 27.9 1.0 CG A:ASP11 4.8 29.9 1.0 OD1 A:ASP154 4.8 30.9 1.0 O3G A:ATP400 4.8 28.1 1.0 OD2 A:ASP154 4.9 29.6 1.0 O2A A:ATP400 4.9 26.7 1.0 CG A:GLN137 4.9 28.5 1.0 O2B A:ATP400 5.0 27.5 1.0 CE A:LYS18 5.0 29.7 1.0

Calcium binding site 2 out of 2 in the Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Actin Dimer Cross-Linked Between Residues 41 and 374 and Proteolytically Cleaved By Subtilisin Between Residues 47 and 48. within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:27.0 occ:1.00 O2G B:ATP400 2.3 28.1 1.0 O1B B:ATP400 2.5 27.1 1.0 O B:HOH413 3.3 7.0 1.0 OE1 B:GLN137 3.5 27.6 1.0 PG B:ATP400 3.6 27.8 1.0 PB B:ATP400 3.8 26.4 1.0 O1A B:ATP400 3.8 29.0 1.0 CD B:GLN137 4.0 28.7 1.0 O B:HOH410 4.0 2.2 1.0 O1G B:ATP400 4.0 27.9 1.0 O3B B:ATP400 4.2 26.2 1.0 O3A B:ATP400 4.2 27.3 1.0 NE2 B:GLN137 4.3 28.6 1.0 OD2 B:ASP11 4.3 29.8 1.0 CA B:GLY13 4.4 27.9 1.0 OD1 B:ASP11 4.5 31.1 1.0 NZ B:LYS18 4.5 29.0 1.0 PA B:ATP400 4.5 27.6 1.0 CG2 B:VAL339 4.6 27.9 1.0 OD1 B:ASP154 4.7 31.0 1.0 OD2 B:ASP154 4.8 29.6 1.0 O3G B:ATP400 4.8 28.1 1.0 CG B:ASP11 4.8 30.0 1.0 CG B:GLN137 4.9 28.5 1.0 O2A B:ATP400 5.0 26.7 1.0

M.R.Sawaya, D.S.Kudryashov, I.Pashkov, H.Adisetiyo, E.Reisler, T.O.Yeates. Multiple Crystal Structures of Actin Dimers and Their Implications For Interactions in the Actin Filament. Acta Crystallogr.,Sect.D V. 64 454 2008.
ISSN: ISSN 0907-4449
PubMed: 18391412
DOI: 10.1107/S0907444908003351