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Zinc in PDB 6qfx: Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) to Generate An Artificial Transfer Hydrogenase (Athase)

Enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) to Generate An Artificial Transfer Hydrogenase (Athase)

All present enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) 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 10) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfx 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) 41.02 / 1.32
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.348, 41.587, 72.471, 90.00, 104.38, 90.00
R / Rfree (%) 17.2 / 19.7

Other elements in 6qfx:

The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) 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 10) to Generate An Artificial Transfer Hydrogenase (Athase) (pdb code 6qfx). 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 10) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfx:

Zinc binding site 1 out of 1 in 6qfx

Go back to Zinc Binding Sites List in 6qfx
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) 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 10) to Generate An Artificial Transfer Hydrogenase (Athase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:14.1
occ:1.00
 N3 A:JR3301 1.9 12.8 1.0
NE2 A:HIS94 2.0 16.1 1.0
ND1 A:HIS119 2.0 13.1 1.0
NE2 A:HIS96 2.0 14.7 1.0
CE1 A:HIS119 2.9 12.2 1.0
CD2 A:HIS94 3.0 15.1 1.0
O2 A:JR3301 3.0 24.2 1.0
S1 A:JR3301 3.0 24.5 1.0
CD2 A:HIS96 3.0 13.6 1.0
CE1 A:HIS94 3.0 14.5 1.0
CE1 A:HIS96 3.1 15.2 1.0
CG A:HIS119 3.1 13.6 1.0
CB A:HIS119 3.6 13.4 1.0
O A:HOH549 3.7 27.1 1.0
OG1 A:THR198 3.8 14.5 1.0
OE1 A:GLU106 4.0 15.6 1.0
O1 A:JR3301 4.1 19.5 1.0
NE2 A:HIS119 4.1 13.2 1.0
C10 A:JR3301 4.1 27.4 1.0
ND1 A:HIS94 4.2 14.3 1.0
CG A:HIS94 4.2 14.2 1.0
CD2 A:HIS119 4.2 12.0 1.0
CG A:HIS96 4.2 14.0 1.0
ND1 A:HIS96 4.2 14.6 1.0
O A:HOH597 4.6 40.8 1.0
C9 A:JR3301 4.8 28.8 1.0
CD A:GLU106 4.9 16.8 1.0
C11 A:JR3301 5.0 27.0 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 05:39:05 2024

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