Magnesium in PDB 5eqn: Structure of Phosphonate Hydroxylase

The structure of Structure of Phosphonate Hydroxylase, PDB code: 5eqn was solved by C.Li, Y.Hu, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.20 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.880, 95.090, 138.240, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 24.1

The binding sites of Magnesium atom in the Structure of Phosphonate Hydroxylase (pdb code 5eqn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Phosphonate Hydroxylase, PDB code: 5eqn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Phosphonate Hydroxylase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Phosphonate Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:27.7 occ:1.00 NE2 A:HIS150 2.5 25.9 1.0 NE2 A:HIS288 2.6 26.7 1.0 OD2 A:ASP152 3.1 56.7 1.0 CE1 A:HIS150 3.2 28.8 1.0 CD2 A:HIS288 3.4 22.9 1.0 CD2 A:HIS150 3.6 21.2 1.0 NH1 A:ARG309 3.6 59.1 1.0 CE1 A:HIS288 3.7 24.0 1.0 CG A:ASP152 4.1 59.4 1.0 OD1 A:ASP152 4.3 61.3 1.0 ND1 A:HIS150 4.4 26.4 1.0 CD A:ARG309 4.6 44.7 1.0 CG A:HIS150 4.6 20.2 1.0 CG A:HIS288 4.6 24.3 1.0 O A:HOH539 4.7 38.4 1.0 ND1 A:HIS288 4.8 26.9 1.0 CZ A:ARG309 4.8 56.4 1.0

Magnesium binding site 2 out of 2 in the Structure of Phosphonate Hydroxylase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Phosphonate Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:31.5 occ:1.00 NE2 B:HIS150 2.6 28.6 1.0 NE2 B:HIS288 2.6 25.7 1.0 OD2 B:ASP152 2.7 59.6 1.0 O B:HOH572 2.8 30.7 1.0 O B:HOH511 2.8 47.0 1.0 CE1 B:HIS150 3.5 27.4 1.0 CE1 B:HIS288 3.5 26.9 1.0 CD2 B:HIS150 3.6 26.7 1.0 CD2 B:HIS288 3.6 24.9 1.0 CG B:ASP152 3.9 54.6 1.0 NH1 B:ARG309 3.9 47.8 1.0 OD1 B:ASP152 4.4 54.0 1.0 O B:HOH517 4.5 55.6 1.0 CD B:ARG309 4.5 35.4 1.0 ND1 B:HIS150 4.6 27.2 1.0 ND1 B:HIS288 4.7 25.8 1.0 CG B:HIS150 4.7 23.9 1.0 CG B:HIS288 4.8 26.9 1.0

C.Li, M.Junaid, E.A.Almuqri, S.Hao, H.Zhang. Structural Analysis of A Phosphonate Hydroxylase with An Access Tunnel at the Back of the Active Site. Acta Crystallogr.,Sect.F V. 72 362 2016.
ISSN: ESSN 2053-230X
PubMed: 27139827
DOI: 10.1107/S2053230X16004933