Calcium in PDB 4o1q: Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q was solved by E.T.Yukl, C.W.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.49 / 2.59
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	55.530, 83.520, 107.780, 109.94, 91.54, 105.78
R / Rfree (%)	19.8 / 25.4

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Iron	(Fe)	4 atoms
Sodium	(Na)	1 atom

The binding sites of Calcium atom in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 4o1q). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:61.2 occ:1.00 O A:HOH550 2.1 46.3 1.0 O A:THR275 2.3 49.6 1.0 O A:HOH534 2.4 46.5 1.0 O A:PRO277 2.5 49.3 1.0 OD1 A:ASN66 2.5 51.3 1.0 C A:THR275 3.5 50.4 1.0 CG A:ASN66 3.6 51.9 1.0 C A:PRO277 3.7 50.2 1.0 OG1 A:THR275 4.0 48.0 1.0 O A:THR67 4.1 50.3 1.0 CB A:THR275 4.1 48.8 1.0 O2A A:HEC403 4.2 46.4 1.0 C A:GLY276 4.2 52.2 1.0 ND2 A:ASN66 4.2 53.1 1.0 CA A:GLY276 4.3 51.9 1.0 N A:GLY276 4.4 51.5 1.0 CA A:TYR278 4.4 48.4 1.0 O A:GLY276 4.4 52.4 1.0 N A:PRO277 4.4 52.3 1.0 CA A:THR275 4.5 50.3 1.0 N A:TYR278 4.5 49.8 1.0 CD1 A:TYR278 4.6 48.0 1.0 O1A A:HEC403 4.7 45.6 1.0 CA A:PRO277 4.7 51.9 1.0 CGA A:HEC403 4.7 46.0 1.0 CB A:ASN66 4.8 51.6 1.0 CE1 A:TYR278 5.0 48.6 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca401 b:33.5 occ:1.00 O B:HOH542 2.2 17.5 1.0 O B:HOH548 2.3 22.7 1.0 OD1 B:ASN66 2.3 41.3 1.0 O B:PRO277 2.3 37.6 1.0 O B:THR275 2.3 38.9 1.0 O B:HOH551 2.5 26.4 1.0 O B:HOH584 2.8 29.5 1.0 CG B:ASN66 3.3 42.0 1.0 C B:THR275 3.3 39.1 1.0 C B:PRO277 3.5 38.3 1.0 C B:GLY276 3.7 40.2 1.0 CA B:GLY276 3.8 39.6 1.0 ND2 B:ASN66 3.8 43.2 1.0 O B:GLY276 3.9 40.5 1.0 N B:GLY276 4.0 39.6 1.0 N B:PRO277 4.1 40.2 1.0 CB B:THR275 4.3 38.2 1.0 O B:THR67 4.3 40.9 1.0 O B:HOH555 4.4 32.8 1.0 N B:TYR278 4.4 37.9 1.0 CA B:TYR278 4.4 36.8 1.0 CA B:THR275 4.4 39.3 1.0 CA B:PRO277 4.4 39.7 1.0 OG1 B:THR275 4.5 37.8 1.0 O1A B:HEC403 4.5 37.4 1.0 CB B:ASN66 4.5 41.7 1.0 O2A B:HEC403 4.6 37.6 1.0 CD B:PRO277 4.7 41.0 1.0 CD1 B:TYR278 4.8 36.6 1.0 CGA B:HEC403 4.9 37.3 1.0 O B:HOH595 5.0 21.7 0.5

S.Shin, E.T.Yukl, E.Sehanobish, C.M.Wilmot, V.L.Davidson. Site-Directed Mutagenesis of GLN103 Reveals the Influence of This Residue on the Redox Properties and Stability of Maug. Biochemistry V. 53 1342 2014.
ISSN: ISSN 0006-2960
PubMed: 24517455
DOI: 10.1021/BI5000349