Sodium in PDB 9fbp: Deletion Mutant MMCHI60

All present enzymatic activity of Deletion Mutant MMCHI60:
3.2.1.14;

The structure of Deletion Mutant MMCHI60, PDB code: 9fbp was solved by W.Rypniewski, M.Bejger, K.Biniek-Antosiak, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.09 / 1.84
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.79, 172.829, 47.088, 90, 90.01, 90
R / Rfree (%)	15.5 / 21.9

The binding sites of Sodium atom in the Deletion Mutant MMCHI60 (pdb code 9fbp). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Deletion Mutant MMCHI60, PDB code: 9fbp:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Deletion Mutant MMCHI60


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Deletion Mutant MMCHI60 within 5.0Å range: probe atom residue distance (Å) B Occ A:Na401 b:26.1 occ:1.00 O A:GLY144 2.3 24.9 1.0 OD1 A:ASN105 2.3 21.1 1.0 OD1 A:ASP146 2.3 20.3 1.0 O A:THR24 2.4 28.5 1.0 O A:HOH569 2.8 35.8 1.0 CG A:ASP146 3.2 19.7 1.0 C A:GLY144 3.2 19.9 1.0 CG A:ASN105 3.3 23.0 1.0 C A:THR24 3.4 27.5 1.0 OD2 A:ASP146 3.5 19.0 1.0 ND2 A:ASN105 3.7 18.8 1.0 O A:PHE145 3.8 20.5 1.0 CA A:GLY144 3.9 20.0 1.0 CA A:ILE25 4.0 28.0 1.0 C A:PHE145 4.0 18.9 1.0 N A:ILE25 4.1 28.1 1.0 N A:THR24 4.2 33.8 1.0 N A:PHE145 4.2 20.5 1.0 N A:THR26 4.2 25.5 1.0 N A:ASP146 4.3 18.1 1.0 OG1 A:THR26 4.3 29.0 1.0 CA A:THR24 4.4 30.8 1.0 CB A:ASP146 4.4 20.0 1.0 CA A:ASP146 4.5 18.6 1.0 CA A:PHE145 4.5 18.3 1.0 CB A:ASN105 4.6 21.4 1.0 C A:ILE25 4.6 24.2 1.0 CG2 A:ILE101 4.8 25.1 1.0 CB A:THR26 4.8 24.6 1.0 N A:GLY23 4.8 42.0 1.0

Sodium binding site 2 out of 2 in the Deletion Mutant MMCHI60


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Deletion Mutant MMCHI60 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na401 b:24.3 occ:1.00 O B:GLY144 2.1 23.4 1.0 OD1 B:ASP146 2.2 18.9 1.0 OD1 B:ASN105 2.2 24.8 1.0 O B:THR24 2.6 52.5 1.0 O B:HOH512 2.9 35.0 1.0 CG B:ASP146 3.1 20.0 1.0 CG B:ASN105 3.1 27.4 1.0 C B:GLY144 3.3 19.8 1.0 OD2 B:ASP146 3.4 18.4 1.0 ND2 B:ASN105 3.5 21.9 1.0 C B:THR24 3.6 41.4 1.0 O B:PHE145 3.9 20.2 1.0 CA B:GLY144 4.0 25.1 1.0 C B:PHE145 4.0 22.7 1.0 N B:THR26 4.1 28.8 1.0 CA B:ILE25 4.2 35.2 1.0 N B:ILE25 4.3 36.7 1.0 N B:PHE145 4.3 22.1 1.0 N B:ASP146 4.4 19.5 1.0 CB B:ASN105 4.4 27.4 1.0 CB B:ASP146 4.4 17.6 1.0 OG1 B:THR26 4.4 25.1 1.0 CG2 B:ILE101 4.5 21.1 1.0 N B:THR24 4.5 36.9 1.0 CA B:PHE145 4.6 18.9 1.0 CA B:ASP146 4.6 18.6 1.0 CB B:THR26 4.6 27.8 1.0 C B:ILE25 4.6 30.9 1.0 CA B:THR24 4.7 45.8 1.0 N B:GLY23 4.9 37.6 1.0 CA B:THR26 5.0 27.8 1.0

M.Bejger, P.H.Malecki, K.Biniek-Antosiak, W.Rypniewski. Probing the Structure and Thermodynamics of A Psychrophilic Chitinase To Be Published.