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Chromium 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:

Sodium (Na) 2 atoms

Chromium Binding Sites:

The binding sites of Chromium 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 Chromium atom.
In total 2 binding sites of Chromium 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 Chromium binding site number: 1; 2;

Chromium binding site 1 out of 2 in 2z68

Go back to Chromium Binding Sites List in 2z68
Chromium 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 Chromium with other atoms in the Cr 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:Cr901

b:19.6
occ:1.00
 CR A:TIL901 0.0 19.6 1.0
OB A:TIL901 1.8 16.2 1.0
OA A:TIL901 1.9 19.6 1.0
NB A:TIL901 1.9 19.4 1.0
OE2 A:GLU24 2.0 21.9 1.0
O A:HOH1115 2.1 19.4 1.0
NE2 A:HIS20 2.1 17.2 1.0
CC1 A:TIL901 2.8 18.5 1.0
CC2 A:TIL901 2.8 18.4 1.0
CB A:TIL901 2.8 17.1 1.0
CB2 A:TIL901 2.9 16.3 1.0
CE1 A:HIS20 3.1 16.8 1.0
CD A:GLU24 3.1 22.3 1.0
CD2 A:HIS20 3.1 16.1 1.0
CB1 A:TIL901 3.3 14.9 1.0
CG A:GLU24 3.6 18.8 1.0
O A:HOH1049 4.0 30.3 1.0
CC6 A:TIL901 4.1 20.2 1.0
CC3 A:TIL901 4.1 18.8 1.0
CB3 A:TIL901 4.2 15.9 1.0
OE1 A:GLU24 4.2 24.2 1.0
ND1 A:HIS20 4.2 17.1 1.0
CG A:HIS20 4.3 17.3 1.0
O A:HOH1037 4.3 33.5 1.0
CE2 A:PHE201 4.6 17.4 1.0
CB6 A:TIL901 4.7 15.5 1.0
O A:HOH1116 4.8 39.6 1.0

Chromium binding site 2 out of 2 in 2z68

Go back to Chromium Binding Sites List in 2z68
Chromium 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 Chromium with other atoms in the Cr 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:Cr902

b:20.2
occ:1.00
 CR B:TIL902 0.0 20.2 1.0
OB B:TIL902 1.8 25.9 1.0
OA B:TIL902 1.8 32.0 1.0
NB B:TIL902 1.9 26.7 1.0
OE2 B:GLU24 2.1 27.1 1.0
O B:HOH1117 2.1 22.7 1.0
NE2 B:HIS20 2.1 15.1 1.0
CC1 B:TIL902 2.7 28.1 1.0
CC2 B:TIL902 2.7 26.7 1.0
CB B:TIL902 2.9 21.0 1.0
CB2 B:TIL902 2.9 23.7 1.0
CE1 B:HIS20 3.1 17.1 1.0
CD B:GLU24 3.1 28.4 1.0
CD2 B:HIS20 3.1 16.7 1.0
CB1 B:TIL902 3.3 22.0 1.0
CG B:GLU24 3.5 24.9 1.0
CC6 B:TIL902 4.0 31.0 1.0
CC3 B:TIL902 4.1 28.0 1.0
CB3 B:TIL902 4.2 24.9 1.0
ND1 B:HIS20 4.2 17.1 1.0
OE1 B:GLU24 4.2 28.9 1.0
O B:HOH947 4.2 28.7 1.0
CG B:HIS20 4.2 17.8 1.0
CE2 B:PHE201 4.6 13.7 1.0
CB6 B:TIL902 4.7 22.7 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: Sun Dec 13 10:55:12 2020

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