Sodium in PDB 4qop: Structure of Bacillus Pumilus Catalase with Hydroquinone Bound.

All present enzymatic activity of Structure of Bacillus Pumilus Catalase with Hydroquinone Bound.:
1.11.1.6;

The structure of Structure of Bacillus Pumilus Catalase with Hydroquinone Bound., PDB code: 4qop was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	104.13 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	92.279, 109.455, 104.199, 90.00, 92.05, 90.00
R / Rfree (%)	23 / 26.1

The structure of Structure of Bacillus Pumilus Catalase with Hydroquinone Bound. also contains other interesting chemical elements:

Iron	(Fe)	8 atoms
Chlorine	(Cl)	6 atoms

The binding sites of Sodium atom in the Structure of Bacillus Pumilus Catalase with Hydroquinone Bound. (pdb code 4qop). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Structure of Bacillus Pumilus Catalase with Hydroquinone Bound., PDB code: 4qop:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Structure of Bacillus Pumilus Catalase with Hydroquinone Bound.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Bacillus Pumilus Catalase with Hydroquinone Bound. within 5.0Å range: probe atom residue distance (Å) B Occ A:Na506 b:12.8 occ:1.00 O A:HOH837 1.7 26.3 1.0 O A:HOH835 1.8 21.3 1.0 O A:HOH836 1.9 28.1 1.0 O A:HOH834 2.2 34.9 1.0 OG A:SER72 2.2 32.7 1.0 OE2 A:GLU85 2.3 36.2 1.0 CD A:GLU85 3.1 37.7 1.0 OE1 A:GLU85 3.2 39.3 1.0 CB A:SER72 3.3 32.4 1.0 O A:HOH838 3.8 40.2 1.0 N A:SER72 3.8 32.8 1.0 CA A:SER72 4.0 32.6 1.0 OE2 A:GLU74 4.0 35.5 1.0 OE1 A:GLU74 4.1 42.4 1.0 O A:SER72 4.1 28.2 1.0 C A:SER72 4.4 32.1 1.0 CD A:GLU74 4.5 37.8 1.0 CG A:GLU85 4.6 38.8 1.0 C A:ASN71 4.9 33.6 1.0

Sodium binding site 2 out of 2 in the Structure of Bacillus Pumilus Catalase with Hydroquinone Bound.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of Bacillus Pumilus Catalase with Hydroquinone Bound. within 5.0Å range: probe atom residue distance (Å) B Occ B:Na505 b:25.9 occ:1.00 OE2 B:GLU85 2.2 52.1 1.0 O B:HOH924 2.3 36.2 1.0 OG B:SER72 2.4 32.7 1.0 OE1 B:GLU85 3.0 47.9 1.0 CD B:GLU85 3.0 42.8 1.0 CB B:SER72 3.4 34.2 1.0 N B:SER72 4.0 31.2 1.0 OE2 B:GLU74 4.2 37.3 1.0 CA B:SER72 4.2 33.5 1.0 OE1 B:GLU74 4.3 37.5 1.0 CG B:GLU85 4.4 41.4 1.0 O B:SER72 4.5 37.6 1.0 CD B:GLU74 4.7 38.4 1.0 C B:SER72 4.8 34.7 1.0

P.C.Loewen, J.Villanueva, J.Switala, L.J.Donald, A.Ivancich. Unprecedented Access of Phenolic Substrates to the Heme Active Site of A Catalase: Substrate Binding and Peroxidase-Like Reactivity of Bacillus Pumilus Catalase Monitored By X-Ray Crystallography and Epr Spectroscopy. Proteins 2015.
ISSN: ESSN 1097-0134
PubMed: 25663126
DOI: 10.1002/PROT.24777