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Calcium in PDB 3rmz: Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rmz was solved by L.M.R.Jensen, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.58 / 1.72
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.527, 83.524, 107.782, 109.94, 91.54, 105.78
R / Rfree (%) 13.8 / 18.1

Other elements in 3rmz:

The structure of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

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

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3rmz). 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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rmz:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 3rmz

Go back to Calcium Binding Sites List in 3rmz
Calcium binding site 1 out of 2 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca400

b:14.6
occ:1.00
O A:HOH396 2.3 10.8 1.0
O A:PRO277 2.3 13.8 1.0
OD1 A:ASN66 2.3 15.2 1.0
O A:HOH387 2.4 9.2 1.0
O A:HOH380 2.4 7.9 1.0
O A:THR275 2.4 16.2 1.0
O A:HOH378 2.5 10.0 1.0
CG A:ASN66 3.4 12.8 1.0
C A:PRO277 3.6 13.3 1.0
C A:THR275 3.6 15.0 1.0
ND2 A:ASN66 4.0 13.1 1.0
C A:GLY276 4.1 15.8 1.0
N A:PRO277 4.3 16.4 1.0
O A:HOH425 4.3 12.2 1.0
O A:THR67 4.4 13.6 1.0
CA A:TYR278 4.4 12.6 1.0
CB A:THR275 4.4 15.2 1.0
CA A:GLY276 4.4 14.0 1.0
OG1 A:THR275 4.4 14.8 1.0
O A:GLY276 4.4 16.4 1.0
N A:TYR278 4.4 14.2 1.0
N A:GLY276 4.5 14.4 1.0
O1A A:HEC600 4.5 15.9 1.0
O A:HOH398 4.6 10.2 1.0
CA A:PRO277 4.6 15.3 1.0
CB A:ASN66 4.6 12.0 1.0
CA A:THR275 4.7 15.3 1.0
O2A A:HEC600 4.7 15.8 1.0
CD2 A:TYR278 4.8 14.8 1.0
CD A:PRO277 4.9 17.1 1.0

Calcium binding site 2 out of 2 in 3rmz

Go back to Calcium Binding Sites List in 3rmz
Calcium binding site 2 out of 2 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca400

b:13.7
occ:1.00
O B:PRO277 2.3 14.3 1.0
O B:HOH383 2.3 10.0 1.0
O B:HOH417 2.4 10.5 1.0
OD1 B:ASN66 2.4 12.6 1.0
O B:THR275 2.4 14.9 1.0
O B:HOH399 2.4 9.3 1.0
O B:HOH443 2.5 10.9 1.0
CG B:ASN66 3.5 13.7 1.0
C B:PRO277 3.5 13.9 1.0
C B:THR275 3.6 14.2 1.0
ND2 B:ASN66 4.0 15.1 1.0
C B:GLY276 4.0 15.2 1.0
N B:PRO277 4.2 15.0 1.0
O B:HOH439 4.3 12.7 1.0
CB B:THR275 4.3 16.1 1.0
CA B:GLY276 4.4 14.2 1.0
O B:THR67 4.4 15.3 1.0
CA B:TYR278 4.4 11.5 1.0
OG1 B:THR275 4.4 13.9 1.0
N B:TYR278 4.4 13.7 1.0
O B:GLY276 4.4 15.9 1.0
N B:GLY276 4.5 13.8 1.0
CA B:PRO277 4.5 15.1 1.0
O1A B:HEC600 4.5 13.2 1.0
O B:HOH475 4.6 10.7 1.0
CA B:THR275 4.6 14.8 1.0
CB B:ASN66 4.7 12.1 1.0
O2A B:HEC600 4.7 14.1 1.0
CD2 B:TYR278 4.8 13.2 1.0
O B:HOH423 4.9 17.7 1.0
CD B:PRO277 5.0 14.7 1.0

Reference:

N.A.Tarboush, L.M.Jensen, E.T.Yukl, J.Geng, A.Liu, C.M.Wilmot, V.L.Davidson. Mutagenesis of TRYPTOPHAN199 Suggests That Hopping Is Required For Maug-Dependent Tryptophan Tryptophylquinone Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 108 16956 2011.
ISSN: ISSN 0027-8424
PubMed: 21969534
DOI: 10.1073/PNAS.1109423108
Page generated: Tue Jul 8 16:21:51 2025

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