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Iridium in PDB 6qfv: Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase)

Enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase)

All present enzymatic activity of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) 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 8) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfv 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) 41.10 / 1.45
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.396, 41.680, 72.353, 90.00, 104.40, 90.00
R / Rfree (%) 15.6 / 16.7

Other elements in 6qfv:

The structure of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Zinc (Zn) 1 atom

Iridium Binding Sites:

The binding sites of Iridium atom in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase) (pdb code 6qfv). This binding sites where shown within 5.0 Angstroms radius around Iridium atom.
In total only one binding site of Iridium was determined in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfv:

Iridium binding site 1 out of 1 in 6qfv

Go back to Iridium Binding Sites List in 6qfv
Iridium binding site 1 out of 1 in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase)


Mono view


Stereo pair view

A full contact list of Iridium with other atoms in the Ir binding site number 1 of Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 8) to Generate An Artificial Transfer Hydrogenase (Athase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ir301

b:16.7
occ:0.90
 IR1 A:J0N301 0.0 16.7 0.9
N1 A:J0N301 2.0 19.8 1.0
N2 A:J0N301 2.1 15.2 1.0
C14 A:J0N301 2.1 20.4 0.9
C13 A:J0N301 2.1 19.9 1.0
C17 A:J0N301 2.1 18.3 0.9
C15 A:J0N301 2.1 16.4 0.9
C16 A:J0N301 2.2 18.2 0.9
CL1 A:J0N301 2.4 38.1 0.9
C6 A:J0N301 2.9 19.0 1.0
C5 A:J0N301 2.9 18.8 1.0
C1 A:J0N301 3.0 23.8 1.0
C21 A:J0N301 3.2 19.5 0.9
C22 A:J0N301 3.3 19.5 0.9
C19 A:J0N301 3.3 19.3 0.9
C23 A:J0N301 3.3 16.2 1.0
C18 A:J0N301 3.3 17.6 0.9
C20 A:J0N301 3.4 20.8 0.9
C24 A:J0N301 4.0 16.6 1.0
O3 A:J0N301 4.2 22.3 1.0
CE2 A:PHE130 4.2 16.1 1.0
C2 A:J0N301 4.3 22.2 1.0
C4 A:J0N301 4.4 23.4 1.0
CD2 A:PHE130 4.7 16.4 1.0
C3 A:J0N301 4.8 26.6 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: Mon Aug 12 03:42:08 2024

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