Calcium in PDB 5lbi: Apo-Structure of Humanised Rada-Mutant HUMRADA3

The structure of Apo-Structure of Humanised Rada-Mutant HUMRADA3, PDB code: 5lbi was solved by M.Marsh, G.Fischer, T.Moschetti, T.Sharpe, D.Scott, M.Morgan, H.Ng, J.Skidmore, A.Venkitaraman, C.Abell, T.L.Blundell, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.30 / 1.43
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.350, 77.980, 39.810, 90.00, 117.53, 90.00
R / Rfree (%)	16.4 / 19.3

The binding sites of Calcium atom in the Apo-Structure of Humanised Rada-Mutant HUMRADA3 (pdb code 5lbi). 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 Apo-Structure of Humanised Rada-Mutant HUMRADA3, PDB code: 5lbi:

Calcium binding site 1 out of 1 in the Apo-Structure of Humanised Rada-Mutant HUMRADA3


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Apo-Structure of Humanised Rada-Mutant HUMRADA3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:14.2 occ:1.00 H A:GLY143 2.3 10.4 1.0 H A:THR145 2.4 8.7 1.0 H A:GLN146 2.5 5.2 1.0 HB A:THR145 2.8 9.2 1.0 HG2 A:GLN146 2.8 8.7 1.0 HA2 A:GLY143 3.0 7.6 1.0 O A:HOH601 3.1 17.3 1.0 N A:GLY143 3.2 9.9 1.0 O A:HOH703 3.2 33.6 1.0 N A:THR145 3.3 7.5 1.0 CA A:GLY143 3.3 9.3 1.0 HA2 A:GLY141 3.4 14.4 1.0 C A:GLY143 3.4 10.2 1.0 O A:HOH652 3.4 31.3 1.0 N A:GLN146 3.4 7.5 1.0 H A:LYS144 3.5 6.9 1.0 N A:LYS144 3.5 7.5 1.0 HG2 A:LYS144 3.6 9.8 1.0 H A:GLY141 3.7 16.3 1.0 CB A:THR145 3.8 10.7 1.0 CG A:GLN146 3.8 11.0 1.0 CA A:THR145 3.9 8.1 1.0 HB2 A:GLN146 3.9 6.7 1.0 O A:GLY143 4.0 9.1 1.0 CA A:GLY141 4.0 15.1 1.0 C A:GLY141 4.0 18.5 1.0 C A:THR145 4.1 8.7 1.0 N A:SER142 4.1 13.2 1.0 HE21 A:GLN146 4.2 30.3 1.0 H A:SER142 4.2 12.0 1.0 C A:LYS144 4.2 7.2 1.0 CB A:GLN146 4.3 8.7 1.0 N A:GLY141 4.3 15.1 1.0 HG3 A:GLN146 4.3 10.9 1.0 CA A:LYS144 4.4 6.8 1.0 C A:SER142 4.4 11.7 1.0 HA3 A:GLY143 4.4 7.9 1.0 HG A:SER142 4.4 9.7 1.0 OG1 A:THR145 4.4 11.4 1.0 CA A:GLN146 4.5 6.8 1.0 O A:GLY141 4.5 17.4 1.0 CG A:LYS144 4.5 10.2 1.0 HG3 A:LYS144 4.6 11.7 1.0 HD13 A:ILE342 4.6 18.5 1.0 O A:HOH554 4.7 16.4 1.0 CA A:SER142 4.9 12.0 1.0 NE2 A:GLN146 4.9 29.5 1.0 CD A:GLN146 4.9 16.5 1.0 HG22 A:THR145 4.9 11.6 1.0 H A:LEU147 4.9 10.2 1.0 CG2 A:THR145 4.9 10.7 1.0 HA A:THR145 4.9 6.4 1.0

T.Moschetti, T.Sharpe, G.Fischer, M.E.Marsh, H.K.Ng, M.Morgan, D.E.Scott, T.L.Blundell, A.R Venkitaraman, J.Skidmore, C.Abell, M.Hyvonen. Engineering Archeal Surrogate Systems For the Development of Protein-Protein Interaction Inhibitors Against Human RAD51. J.Mol.Biol. V. 428 4589 2016.
ISSN: ESSN 1089-8638
PubMed: 27725183
DOI: 10.1016/J.JMB.2016.10.009