Calcium in PDB 4b1u: Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity.

The structure of Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity., PDB code: 4b1u was solved by S.Mouilleron, M.Wiezlak, N.O'reilly, R.Treisman, N.Q.Mcdonald, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.93 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.600, 77.600, 128.230, 90.00, 90.00, 120.00
R / Rfree (%)	19.5 / 23.6

The structure of Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Calcium atom in the Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity. (pdb code 4b1u). 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 Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity., PDB code: 4b1u:

Calcium binding site 1 out of 1 in the Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the PHACTR1 Rpel Domain and Rpel Motif Directed Assemblies with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity. within 5.0Å range: probe atom residue distance (Å) B Occ M:Ca1163 b:20.9 occ:1.00 N M:LYS134 2.0 34.0 1.0 ND1 M:HIS135 2.1 33.2 0.7 N M:HIS135 2.1 41.5 0.7 N M:HIS135 2.2 41.1 0.3 N M:PHE133 2.2 33.2 1.0 C M:PHE133 2.9 42.6 1.0 C M:LYS134 2.9 41.3 1.0 CA M:LYS134 3.0 37.0 1.0 CG M:HIS135 3.0 36.4 0.7 CA M:PHE133 3.0 33.5 1.0 CA M:HIS135 3.1 40.4 0.7 CE1 M:HIS135 3.1 32.9 0.7 CB M:HIS135 3.2 36.5 0.7 CA M:HIS135 3.2 40.0 0.3 CB M:HIS135 3.4 38.3 0.3 N M:THR136 3.6 38.4 1.0 C M:HIS135 3.8 39.7 0.7 CG M:LYS134 3.9 35.9 1.0 C M:HIS135 4.0 39.4 0.3 CB M:LYS134 4.0 34.8 1.0 O B:HOH2068 4.0 27.1 1.0 O M:PHE133 4.0 34.3 1.0 CD1 M:PHE133 4.1 35.4 1.0 CB M:PHE133 4.1 33.6 1.0 O M:LYS134 4.1 47.6 1.0 CD2 M:HIS135 4.1 33.3 0.7 CG M:PHE133 4.1 33.7 1.0 NE2 M:HIS135 4.2 40.8 0.7 O B:HOH2144 4.3 28.1 1.0 OG1 M:THR136 4.4 33.4 1.0 CD1 B:ILE345 4.7 15.9 1.0 CE1 M:PHE133 4.8 40.3 1.0 CG2 M:THR136 4.9 33.3 1.0 CA M:THR136 4.9 34.0 1.0 O M:HIS135 4.9 34.3 0.7 CD2 M:PHE133 4.9 42.0 1.0 CB M:THR136 5.0 49.2 1.0

S.Mouilleron, M.Wiezlak, N.O'reilly, R.Treisman, N.Q.Mcdonald. Structures of the PHACTR1 Rpel Domain and Rpel Motif Complexes with G-Actin Reveal the Molecular Basis For Actin Binding Cooperativity. Structure V. 20 1960 2012.
ISSN: ISSN 1878-4186
PubMed: 23041370
DOI: 10.1016/J.STR.2012.08.031