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Magnesium in PDB 3b5i: Crystal Structure of Indole-3-Acetic Acid Methyltransferase

Protein crystallography data

The structure of Crystal Structure of Indole-3-Acetic Acid Methyltransferase, PDB code: 3b5i was solved by J.-L.Ferrer, J.P.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.22 / 2.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.270, 129.400, 68.330, 90.00, 112.30, 90.00
R / Rfree (%) 25.7 / 28.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Indole-3-Acetic Acid Methyltransferase (pdb code 3b5i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Indole-3-Acetic Acid Methyltransferase, PDB code: 3b5i:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3b5i

Go back to Magnesium Binding Sites List in 3b5i
Magnesium binding site 1 out of 2 in the Crystal Structure of Indole-3-Acetic Acid Methyltransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Indole-3-Acetic Acid Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:34.7
occ:1.00
O A:PHE268 2.7 52.7 1.0
OD1 A:ASN269 2.8 49.6 1.0
O A:ASN179 2.9 64.0 1.0
O A:ARG265 2.9 73.8 1.0
N A:VAL183 3.1 54.4 1.0
O A:ASP266 3.1 67.7 1.0
C A:ASP266 3.4 67.6 1.0
CA A:VAL183 3.4 52.9 1.0
CA A:ASP266 3.5 69.5 1.0
CG A:ASN269 3.6 48.9 1.0
C A:PHE268 3.8 52.9 1.0
C A:ARG265 3.9 73.8 1.0
ND2 A:ASN269 3.9 49.1 1.0
OD1 A:ASN179 4.0 64.3 1.0
C A:ASN179 4.1 64.1 1.0
CB A:ASN179 4.1 63.9 1.0
N A:ASP266 4.1 71.7 1.0
CG A:ASN179 4.1 63.9 1.0
N A:ARG182 4.2 58.5 1.0
C A:ARG182 4.2 55.8 1.0
N A:PHE268 4.3 56.8 1.0
C A:VAL183 4.3 51.9 1.0
N A:GLY267 4.4 65.0 1.0
CG2 A:VAL183 4.5 52.9 1.0
CB A:VAL183 4.6 52.7 1.0
CA A:PHE268 4.6 54.2 1.0
CA A:ARG182 4.6 56.9 1.0
N A:ASN269 4.7 50.7 1.0
CA A:ASN179 4.7 63.9 1.0
CB A:ASP266 4.7 69.9 1.0
CA A:ASN269 4.8 48.6 1.0
CB A:ASN269 4.8 48.6 1.0
N A:PHE184 4.8 50.5 1.0
N A:GLY181 4.9 62.2 1.0
C A:GLY267 4.9 59.2 1.0
ND2 A:ASN179 4.9 63.9 1.0

Magnesium binding site 2 out of 2 in 3b5i

Go back to Magnesium Binding Sites List in 3b5i
Magnesium binding site 2 out of 2 in the Crystal Structure of Indole-3-Acetic Acid Methyltransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Indole-3-Acetic Acid Methyltransferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:31.2
occ:1.00
O B:ASN179 2.6 64.0 1.0
OD1 B:ASN269 2.8 49.5 1.0
O B:PHE268 3.0 52.7 1.0
O B:ASP266 3.1 67.6 1.0
N B:VAL183 3.3 54.3 1.0
O B:ARG265 3.3 73.8 1.0
C B:ASP266 3.5 67.6 1.0
CG B:ASN269 3.5 49.0 1.0
CA B:ASP266 3.6 69.5 1.0
OD1 B:ASN179 3.6 64.3 1.0
CA B:VAL183 3.7 52.9 1.0
CB B:ASN179 3.8 63.9 1.0
ND2 B:ASN269 3.8 49.5 1.0
C B:ASN179 3.8 64.0 1.0
CG B:ASN179 3.8 63.9 1.0
C B:PHE268 4.0 52.8 1.0
C B:ARG265 4.2 73.8 1.0
N B:ARG182 4.3 58.2 1.0
N B:ASP266 4.3 71.7 1.0
CA B:ASN179 4.3 63.9 1.0
C B:ARG182 4.4 55.8 1.0
N B:PHE268 4.5 56.7 1.0
N B:GLY267 4.5 65.0 1.0
C B:VAL183 4.5 51.9 1.0
ND2 B:ASN179 4.7 64.0 1.0
CB B:ASP266 4.7 69.9 1.0
CA B:ARG182 4.7 56.9 1.0
CB B:ASN269 4.8 48.9 1.0
CA B:ASN269 4.8 48.7 1.0
N B:ASN269 4.8 50.6 1.0
CG2 B:VAL183 4.9 53.0 1.0
CA B:PHE268 4.9 54.3 1.0
N B:PHE184 4.9 50.7 1.0
N B:ARG180 4.9 64.3 1.0
N B:GLY181 4.9 62.2 1.0
CB B:VAL183 4.9 52.7 1.0
N B:ASN179 5.0 63.8 1.0

Reference:

N.Zhao, J.L.Ferrer, J.Ross, J.Guan, Y.Yang, E.Pichersky, J.P.Noel, F.Chen. Structural, Biochemical, and Phylogenetic Analyses Suggest That Indole-3-Acetic Acid Methyltransferase Is An Evolutionarily Ancient Member of the Sabath Family. Plant Physiol. V. 146 455 2008.
ISSN: ISSN 0032-0889
PubMed: 18162595
DOI: 10.1104/PP.107.110049
Page generated: Mon Dec 14 07:54:49 2020

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