Magnesium in PDB 4o4o: Crystal Structure of Phycobiliprotein Lyase Cpct

The structure of Crystal Structure of Phycobiliprotein Lyase Cpct, PDB code: 4o4o was solved by W.Zhou, W.-L.Ding, X.-L.Zeng, L.-L.Dong, B.Zhao, M.Zhou, H.Scheer, K.-H.Zhao, X.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.53 / 1.95
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.322, 69.322, 165.151, 90.00, 90.00, 120.00
R / Rfree (%)	17.3 / 21.4

The binding sites of Magnesium atom in the Crystal Structure of Phycobiliprotein Lyase Cpct (pdb code 4o4o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Phycobiliprotein Lyase Cpct, PDB code: 4o4o:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Phycobiliprotein Lyase Cpct


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Phycobiliprotein Lyase Cpct within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:76.3 occ:1.00 O A:HOH564 2.0 69.6 1.0 O A:HOH563 2.6 65.3 1.0 O A:HOH551 3.3 51.1 1.0 NH2 A:ARG68 3.6 44.7 1.0 NH1 A:ARG66 4.2 85.9 1.0 NH1 A:ARG141 4.2 79.6 1.0 NH2 A:ARG141 4.3 60.7 1.0 CZ A:ARG68 4.6 43.5 1.0 CD A:ARG66 4.6 48.8 1.0 NH1 A:ARG68 4.6 34.1 1.0 O A:HOH466 4.7 46.5 1.0 CG1 A:VAL139 4.7 52.2 1.0 CZ A:ARG141 4.8 71.9 1.0 O A:HOH559 4.9 48.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Phycobiliprotein Lyase Cpct


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Phycobiliprotein Lyase Cpct within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:93.8 occ:1.00 O B:HOH525 2.5 61.7 1.0 O B:HOH475 2.6 55.8 1.0 O B:HOH496 2.8 52.9 1.0 O B:HOH481 2.8 54.9 1.0 O B:HOH524 2.9 61.7 1.0 O B:HOH510 2.9 70.2 1.0 O B:HOH495 3.6 54.6 1.0 OE1 B:GLN55 4.3 53.0 1.0 CD B:GLN55 4.8 51.6 1.0 NE2 B:GLN55 4.9 50.5 1.0

W.Zhou, W.L.Ding, X.L.Zeng, L.L.Dong, B.Zhao, M.Zhou, H.Scheer, K.H.Zhao, X.Yang. Structure and Mechanism of the Phycobiliprotein Lyase Cpct. J.Biol.Chem. V. 289 26677 2014.
ISSN: ISSN 0021-9258
PubMed: 25074932
DOI: 10.1074/JBC.M114.586743