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Zinc in PDB 6qfu: Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase)

Enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase)

All present enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase):
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfu was solved by J.G.Rebelein, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.77 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.038, 41.264, 71.900, 90.00, 104.27, 90.00
R / Rfree (%) 16.5 / 18.6

Other elements in 6qfu:

The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Iridium (Ir) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase) (pdb code 6qfu). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfu:

Zinc binding site 1 out of 1 in 6qfu

Go back to Zinc Binding Sites List in 6qfu
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 7) to Generate An Artificial Transfer Hydrogenase (Athase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:7.6
occ:1.00
 N3 A:J0K301 2.0 8.9 1.0
NE2 A:HIS96 2.0 6.9 1.0
ND1 A:HIS119 2.1 6.7 1.0
NE2 A:HIS94 2.2 7.1 1.0
CD2 A:HIS96 3.0 7.2 1.0
O2 A:J0K301 3.0 10.8 1.0
CE1 A:HIS119 3.0 6.8 1.0
CD2 A:HIS94 3.0 7.1 1.0
S1 A:J0K301 3.1 12.3 1.0
CE1 A:HIS94 3.1 7.2 1.0
CE1 A:HIS96 3.1 7.2 1.0
CG A:HIS119 3.1 6.7 1.0
CB A:HIS119 3.5 6.6 1.0
O A:HOH513 3.6 25.1 1.0
OG1 A:THR198 3.9 7.8 1.0
OE1 A:GLU106 4.0 9.8 1.0
C10 A:J0K301 4.1 12.9 1.0
O1 A:J0K301 4.1 10.6 1.0
CG A:HIS96 4.1 6.6 1.0
NE2 A:HIS119 4.2 6.5 1.0
CG A:HIS94 4.2 6.9 1.0
ND1 A:HIS96 4.2 6.9 1.0
ND1 A:HIS94 4.2 7.2 1.0
CD2 A:HIS119 4.2 6.9 1.0
C9 A:J0K301 4.9 14.4 1.0
CD A:GLU106 4.9 9.4 1.0
C11 A:J0K301 4.9 13.5 1.0
CA A:HIS119 5.0 6.6 1.0

Reference:

J.G.Rebelein, Y.Cotelle, B.Garabedian, T.R.Ward. Chemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase As Host Protein. Acs Catalysis V. 9 4173 2019.
ISSN: ESSN 2155-5435
PubMed: 31080690
DOI: 10.1021/ACSCATAL.9B01006
Page generated: Tue Oct 29 05:37:55 2024

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