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Magnesium in PDB 3ivz: Crystal Structure of Hyperthermophilic Nitrilase

Enzymatic activity of Crystal Structure of Hyperthermophilic Nitrilase

All present enzymatic activity of Crystal Structure of Hyperthermophilic Nitrilase:
3.5.1.6;

Protein crystallography data

The structure of Crystal Structure of Hyperthermophilic Nitrilase, PDB code: 3ivz was solved by J.Raczynska, C.Vorgias, G.Antranikian, W.Rypniewski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.91 / 1.57
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 59.174, 59.174, 127.220, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 17.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Hyperthermophilic Nitrilase (pdb code 3ivz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Hyperthermophilic Nitrilase, PDB code: 3ivz:

Magnesium binding site 1 out of 1 in 3ivz

Go back to Magnesium Binding Sites List in 3ivz
Magnesium binding site 1 out of 1 in the Crystal Structure of Hyperthermophilic Nitrilase


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 Hyperthermophilic Nitrilase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg263

b:22.7
occ:0.70
O A:MET222 2.0 21.8 1.0
O A:HOH285 2.0 25.3 1.0
O A:HOH321 2.1 31.5 1.0
O A:HOH294 2.1 30.2 1.0
O A:HOH314 2.4 27.1 1.0
O A:HOH323 2.4 19.2 0.7
C A:MET222 3.2 21.3 1.0
N A:MET222 4.0 20.6 1.0
CA A:ALA223 4.1 20.8 1.0
OE2 A:GLU229 4.1 31.4 1.0
N A:ALA223 4.1 21.4 1.0
O A:HOH320 4.1 42.0 1.0
CA A:MET222 4.2 21.3 1.0
O A:HOH303 4.3 28.5 1.0
OH A:TYR6 4.3 21.6 1.0
C A:ALA223 4.8 21.7 1.0
OG A:SER221 4.9 19.7 1.0
CB A:MET222 5.0 21.8 1.0

Reference:

J.E.Raczynska, C.E.Vorgias, G.Antranikian, W.Rypniewski. Crystallographic Analysis of A Thermoactive Nitrilase. J.Struct.Biol. V. 173 294 2010.
ISSN: ISSN 1047-8477
PubMed: 21095228
DOI: 10.1016/J.JSB.2010.11.017
Page generated: Mon Dec 14 08:17:40 2020

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