Calcium in PDB 3ue5: Ecp-Cleaved Actin in Complex with Spir Domain D

The structure of Ecp-Cleaved Actin in Complex with Spir Domain D, PDB code: 3ue5 was solved by C.Chen, M.Phillips, M.R.Sawaya, C.Y.Ralston, M.E.Quinlan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.24 / 2.76
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	84.837, 53.551, 100.578, 90.00, 92.65, 90.00
R / Rfree (%)	19.7 / 24

The structure of Ecp-Cleaved Actin in Complex with Spir Domain D also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Calcium atom in the Ecp-Cleaved Actin in Complex with Spir Domain D (pdb code 3ue5). 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 Ecp-Cleaved Actin in Complex with Spir Domain D, PDB code: 3ue5:

Calcium binding site 1 out of 1 in the Ecp-Cleaved Actin in Complex with Spir Domain D


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ecp-Cleaved Actin in Complex with Spir Domain D within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca381 b:37.2 occ:1.00 O A:HOH410 2.1 28.7 1.0 O2G A:ATP382 2.3 31.6 1.0 O1B A:ATP382 2.4 28.6 1.0 O A:HOH397 2.5 38.3 1.0 O A:HOH415 2.7 26.0 1.0 PG A:ATP382 3.6 32.4 1.0 PB A:ATP382 3.7 29.7 1.0 O1G A:ATP382 3.8 32.5 1.0 OE1 A:GLN137 3.9 44.3 1.0 OD1 A:ASP154 4.2 58.6 1.0 O A:HOH408 4.2 30.6 1.0 O1A A:ATP382 4.2 27.9 1.0 OD2 A:ASP154 4.2 50.4 1.0 O3A A:ATP382 4.3 29.1 1.0 OD2 A:ASP11 4.3 53.2 1.0 O3B A:ATP382 4.3 30.1 1.0 CD A:GLN137 4.3 47.8 1.0 O A:HOH380 4.4 23.7 1.0 OD1 A:ASP11 4.5 44.6 1.0 CA A:GLY13 4.5 36.1 1.0 NZ A:LYS18 4.6 25.2 1.0 CG A:ASP154 4.6 52.4 1.0 PA A:ATP382 4.7 27.8 1.0 CG A:GLN137 4.8 37.1 1.0 CG A:ASP11 4.8 44.5 1.0 CG2 A:VAL339 4.8 27.9 1.0 O3G A:ATP382 4.9 32.0 1.0 NE2 A:GLN137 4.9 33.6 1.0 O2B A:ATP382 5.0 29.9 1.0

C.K.Chen, M.R.Sawaya, M.L.Phillips, E.Reisler, M.E.Quinlan. Multiple Forms of Spire-Actin Complexes and Their Functional Consequences. J.Biol.Chem. V. 287 10684 2012.
ISSN: ISSN 0021-9258
PubMed: 22334675
DOI: 10.1074/JBC.M111.317792