Calcium in PDB 6x0h: Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation

All present enzymatic activity of Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation:
1.14.13.196;

The structure of Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation, PDB code: 6x0h was solved by J.J.Tanner, A.C.Campbell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.41 / 2.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	76.765, 156.937, 88.651, 90.00, 110.38, 90.00
R / Rfree (%)	18.2 / 23.2

The binding sites of Calcium atom in the Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation (pdb code 6x0h). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation, PDB code: 6x0h:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca604 b:49.8 occ:1.00 O B:ASP288 2.5 41.5 1.0 OG A:SER138 2.7 28.6 1.0 C B:ASP288 3.7 40.1 1.0 CB A:SER138 3.7 26.7 1.0 O A:ASN136 4.0 21.1 1.0 O A:HOH831 4.0 37.0 1.0 CB B:ASP288 4.2 57.0 1.0 CA B:ASP288 4.4 46.8 1.0 OE2 C:GLU333 4.6 45.3 1.0 N B:SER289 4.7 33.6 1.0 N B:PRO290 4.8 21.3 1.0 C B:SER289 4.8 24.6 1.0 CA B:SER289 4.8 29.9 1.0 CD B:PRO290 4.9 26.3 1.0 C A:ASN136 4.9 22.7 1.0 CA B:PRO290 5.0 22.2 1.0

Calcium binding site 2 out of 2 in the Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of Oxidized Sida Ornithine Hydroxylase with the Fad in the "Out" Conformation within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca603 b:57.3 occ:1.00 O D:ASP288 2.6 48.2 1.0 OG C:SER138 2.7 32.3 1.0 O C:HOH811 2.9 40.9 1.0 CB C:SER138 3.7 26.1 1.0 C D:ASP288 3.8 46.0 1.0 OE2 A:GLU333 4.1 47.7 1.0 O C:ASN136 4.2 32.7 1.0 CB D:ASP288 4.3 58.9 1.0 CA D:ASP288 4.5 47.2 1.0 N D:PRO290 4.8 29.6 1.0 N D:SER289 4.8 39.4 1.0 C D:SER289 4.8 31.0 1.0 CA D:SER289 4.9 35.7 1.0 CA C:SER138 5.0 21.8 1.0

A.C.Campbell, K.M.Stiers, J.S.Martin Del Campo, R.Mehra-Chaudhary, P.Sobrado, J.J.Tanner. Trapping Conformational States of A Flavin-Dependent N -Monooxygenase in Crystallo Reveals Protein and Flavin Dynamics. J.Biol.Chem. V. 295 13239 2020.
ISSN: ESSN 1083-351X
PubMed: 32723870
DOI: 10.1074/JBC.RA120.014750