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Sodium in PDB 2z68: Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase

Enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase

All present enzymatic activity of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase:
1.14.99.3;

Protein crystallography data

The structure of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase, PDB code: 2z68 was solved by N.Yokoi, M.Unno, T.Ueno, M.Ikeda-Saito, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.77 / 1.58
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 40.656, 63.057, 77.964, 90.00, 96.88, 90.00
R / Rfree (%) 17.8 / 22.5

Other elements in 2z68:

The structure of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase also contains other interesting chemical elements:

Chromium (Cr) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase (pdb code 2z68). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase, PDB code: 2z68:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2z68

Go back to Sodium Binding Sites List in 2z68
Sodium binding site 1 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na601

b:70.5
occ:1.00
 OD1 A:ASP174 2.7 31.1 1.0
NH2 A:ARG177 2.9 35.7 1.0
O A:LYS170 3.4 31.6 1.0
CG A:ASP174 3.6 29.7 1.0
CE A:LYS173 3.9 25.8 1.0
OD2 A:ASP174 4.0 32.8 1.0
CB A:LYS173 4.0 22.8 1.0
CZ A:ARG177 4.2 34.0 1.0
N A:ASP174 4.2 25.2 1.0
C A:LYS170 4.3 31.7 1.0
CA A:LYS170 4.4 31.6 1.0
NZ A:LYS173 4.4 26.5 1.0
O A:HOH1114 4.7 43.8 1.0
CB A:LYS170 4.7 31.9 1.0
CB A:ASP174 4.7 27.8 1.0
C A:LYS173 4.7 23.8 1.0
CD A:LYS173 4.7 24.1 1.0
CA A:ASP174 4.8 26.7 1.0
NH1 A:ARG177 4.9 34.9 1.0
CA A:LYS173 4.9 23.3 1.0
CG A:LYS173 5.0 22.9 1.0

Sodium binding site 2 out of 2 in 2z68

Go back to Sodium Binding Sites List in 2z68
Sodium binding site 2 out of 2 in the Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of An Artificial Metalloprotein: Cr[N- Salicylidene-4-Amino-3-Hydroxyhydrocinnamic Acid]/Wild Type Heme Oxygenase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na602

b:41.7
occ:1.00
 O B:HOH1105 1.9 36.8 1.0
O B:HOH983 3.0 19.5 1.0
OE2 B:GLU196 3.1 17.2 1.0
OD1 B:ASP121 3.3 11.2 1.0
CE1 B:HIS192 3.3 12.3 1.0
O A:HOH1013 3.4 23.1 1.0
NE2 B:HIS192 3.5 10.2 1.0
CD B:GLU196 4.0 12.5 1.0
O A:HIS150 4.0 14.3 1.0
CB B:ALA124 4.0 9.8 1.0
O A:HOH987 4.3 26.5 1.0
CD B:ARG112 4.3 14.8 1.0
CA A:TYR151 4.3 13.8 1.0
C A:TYR151 4.3 14.8 1.0
CG1 B:ILE116 4.3 12.0 1.0
OE1 B:GLU196 4.4 17.7 1.0
O A:TYR151 4.4 16.3 1.0
CG B:ASP121 4.4 8.0 1.0
O A:HOH1070 4.5 22.8 1.0
ND1 B:HIS192 4.6 13.1 1.0
NZ B:LYS195 4.8 18.7 0.5
NE B:ARG112 4.8 15.7 1.0
CD2 B:HIS192 4.9 12.1 1.0
N A:GLY152 4.9 14.1 1.0
CD1 B:ILE116 4.9 12.6 1.0
C A:HIS150 4.9 13.7 1.0

Reference:

N.Yokoi, T.Ueno, M.Unno, T.Matsui, M.Ikeda-Saito, Y.Watanabe. Ligand Design For Improvement of Thermal Stabilityof Metal Complex/Protein Hybrids To Be Published.
Page generated: Tue Dec 15 06:00:57 2020

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