Magnesium in PDB 3ki8: Crystal Structure of Hyperthermophilic Nitrilase

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

The structure of Crystal Structure of Hyperthermophilic Nitrilase, PDB code: 3ki8 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)	19.71 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	58.408, 67.151, 59.150, 90.00, 90.82, 90.00
R / Rfree (%)	14.7 / 18.6

The binding sites of Magnesium atom in the Crystal Structure of Hyperthermophilic Nitrilase (pdb code 3ki8). 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 Hyperthermophilic Nitrilase, PDB code: 3ki8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 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:1.00 O A:HOH429 1.9 18.1 1.0 O A:HOH372 2.0 24.4 1.0 O A:HOH430 2.0 22.8 1.0 O A:HOH428 2.0 22.6 1.0 O A:HOH380 2.1 23.1 1.0 O A:HOH431 2.2 29.7 1.0 O A:HOH295 3.8 11.4 1.0 OE2 A:GLU65 4.0 15.3 1.0 O A:HOH303 4.2 21.8 1.0 OD1 A:ASP91 4.3 17.1 1.0 O A:ILE63 4.4 12.8 1.0 OE1 A:GLU65 4.4 14.4 1.0 O A:LYS90 4.7 11.5 1.0 CD A:GLU65 4.7 15.1 1.0 CB A:LYS62 4.8 9.4 1.0 CG A:ASP91 4.8 18.4 1.0 CD A:LYS62 4.9 16.6 1.0 CA A:ASP91 4.9 13.9 1.0 CG A:LYS62 5.0 13.2 1.0

Magnesium binding site 2 out of 2 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 2 of Crystal Structure of Hyperthermophilic Nitrilase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg263 b:23.0 occ:1.00 O B:HOH398 2.0 28.4 1.0 O B:HOH264 2.0 23.5 1.0 O B:HOH323 2.1 28.7 1.0 O B:HOH322 2.2 31.6 1.0 OD1 B:ASN49 2.2 18.5 1.0 O B:HOH324 2.3 30.8 1.0 CG B:ASN49 3.0 15.5 1.0 ND2 B:ASN49 3.2 16.0 1.0 O B:HOH321 3.8 15.6 1.0 O B:HOH325 3.8 36.5 1.0 O B:ACY3003 3.9 26.4 1.0 NE B:ARG119 4.0 12.8 1.0 OXT B:ACY3003 4.3 26.7 1.0 CD B:ARG119 4.4 12.8 1.0 CB B:ASN49 4.5 12.4 1.0 C B:ACY3003 4.5 27.5 1.0 O B:HOH392 4.6 24.9 1.0 O B:PHE50 4.7 13.8 1.0 CZ B:ARG119 4.8 14.0 1.0 O B:ASN49 4.9 13.4 1.0 CA B:ASN49 4.9 12.2 1.0 C B:ASN49 5.0 12.0 1.0 NH1 B:ARG119 5.0 15.8 1.0

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