Calcium in PDB 7jvl: Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation

All present enzymatic activity of Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation:
1.14.13.196;

The structure of Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation, PDB code: 7jvl 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)	62.89 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.229, 153.811, 89.870, 90.00, 109.28, 90.00
R / Rfree (%)	20.4 / 24.1

The binding sites of Calcium atom in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation (pdb code 7jvl). 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 the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation, PDB code: 7jvl:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and 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 the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca605 b:46.5 occ:1.00 O B:ASP288 2.6 32.8 1.0 OD2 B:ASP288 3.0 48.6 1.0 CG B:ASP288 3.4 43.8 1.0 C B:ASP288 3.7 32.3 1.0 OD1 B:ASP288 3.9 42.6 1.0 OG A:SER138 4.0 29.4 1.0 CB B:ASP288 4.0 39.8 1.0 CA B:ASP288 4.4 34.0 1.0 OE2 C:GLU333 4.4 28.2 1.0 CB A:SER138 4.5 20.6 1.0 N B:SER289 4.7 22.1 1.0 O A:ASN136 4.8 17.6 1.0 C B:SER289 4.8 18.8 1.0 N B:PRO290 4.9 19.6 1.0 CA B:SER289 4.9 20.3 1.0

Calcium binding site 2 out of 2 in the Structure of the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and 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 the M101A Variant of the Sida Ornithine Hydroxylase Complexed with Nadp and the Fad in the "Out" Conformation within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca605 b:57.9 occ:1.00 O D:ASP288 2.8 44.4 1.0 OG C:SER138 3.2 29.4 1.0 OD1 D:ASP288 3.3 59.3 1.0 OE2 A:GLU333 4.0 36.9 1.0 CB C:SER138 4.0 23.4 1.0 C D:ASP288 4.0 43.5 1.0 O C:ASN136 4.1 19.7 1.0 O C:HOH791 4.1 26.7 1.0 CG D:ASP288 4.1 54.8 1.0 N D:PRO290 4.6 24.4 1.0 CD D:PRO290 4.6 23.7 1.0 CB D:ASP288 4.7 47.1 1.0 C D:SER289 4.7 25.3 1.0 CA D:SER289 4.8 29.6 1.0 CA D:PRO290 4.8 22.3 1.0 CB D:PRO290 4.8 22.7 1.0 N D:SER289 4.9 30.4 1.0 OD2 D:ASP288 4.9 51.3 1.0 CA D:ASP288 5.0 43.2 1.0

A.C.Campbell, R.Robinson, D.Mena-Aguilar, P.Sobrado, J.J.Tanner. Structural Determinants of Flavin Dynamics in A Class B Monooxygenase. Biochemistry 2020.
ISSN: ISSN 0006-2960
PubMed: 33226785
DOI: 10.1021/ACS.BIOCHEM.0C00783