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Calcium in PDB 3rn0: Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0 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 / 1.91
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 (%) 17.3 / 23

Other elements in 3rn0:

The structure of Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3rn0). 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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 3rn0

Go back to Calcium Binding Sites List in 3rn0
Calcium binding site 1 out of 2 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca400

b:29.7
occ:1.00
OD1 A:ASN66 2.2 29.9 1.0
O A:HOH395 2.3 19.6 1.0
O A:PRO277 2.3 29.6 1.0
O A:HOH377 2.4 11.0 1.0
O A:HOH384 2.4 19.0 1.0
O A:THR275 2.4 34.0 1.0
O A:HOH376 2.5 16.8 1.0
CG A:ASN66 3.4 30.8 1.0
C A:PRO277 3.6 31.1 1.0
C A:THR275 3.7 33.1 1.0
ND2 A:ASN66 3.9 31.6 1.0
C A:GLY276 4.1 32.0 1.0
N A:PRO277 4.2 31.8 1.0
CA A:GLY276 4.3 32.8 1.0
O A:HOH397 4.4 14.8 1.0
O A:HOH421 4.4 11.6 1.0
O A:GLY276 4.4 32.4 1.0
O A:THR67 4.4 26.4 1.0
CA A:TYR278 4.4 30.3 1.0
N A:TYR278 4.4 32.2 1.0
N A:GLY276 4.5 33.3 1.0
CB A:THR275 4.5 32.3 1.0
OG1 A:THR275 4.5 31.9 1.0
CB A:ASN66 4.5 31.9 1.0
O1A A:HEC600 4.6 31.0 1.0
CD A:PRO277 4.6 32.4 1.0
CA A:PRO277 4.6 32.5 1.0
CA A:THR275 4.7 33.0 1.0
CD2 A:TYR278 4.9 27.4 1.0
O A:HOH443 4.9 19.1 1.0
O2A A:HEC600 4.9 29.4 1.0

Calcium binding site 2 out of 2 in 3rn0

Go back to Calcium Binding Sites List in 3rn0
Calcium binding site 2 out of 2 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca400

b:20.3
occ:1.00
O B:PRO277 2.2 19.7 1.0
O B:HOH383 2.3 16.8 1.0
O B:THR275 2.3 21.4 1.0
O B:HOH431 2.4 18.9 1.0
OD1 B:ASN66 2.5 23.0 1.0
O B:HOH414 2.6 15.6 1.0
O B:HOH399 2.6 18.2 1.0
CG B:ASN66 3.5 22.9 1.0
C B:PRO277 3.5 23.7 1.0
C B:THR275 3.5 24.7 1.0
ND2 B:ASN66 3.9 21.3 1.0
C B:GLY276 3.9 25.3 1.0
N B:PRO277 4.1 26.2 1.0
O B:HOH437 4.2 22.0 1.0
CA B:GLY276 4.2 24.3 1.0
OG1 B:THR275 4.2 22.6 1.0
O B:GLY276 4.3 26.5 1.0
CB B:THR275 4.3 24.7 1.0
N B:GLY276 4.3 22.5 1.0
O B:THR67 4.3 22.7 1.0
N B:TYR278 4.4 19.8 1.0
CA B:TYR278 4.4 21.6 1.0
O B:HOH461 4.5 16.7 1.0
O1A B:HEC600 4.5 17.1 1.0
CA B:PRO277 4.5 23.5 1.0
CA B:THR275 4.6 25.8 1.0
CD2 B:TYR278 4.7 20.6 1.0
CB B:ASN66 4.8 22.8 1.0
O2A B:HEC600 4.8 21.7 1.0
O B:HOH421 4.8 21.5 1.0
CD B:PRO277 4.9 26.7 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 16:22:21 2025

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