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Iridium in PDB 7onv: Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)

Enzymatic activity of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase)

All present enzymatic activity of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase):
4.2.1.1; 4.2.1.69;

Protein crystallography data

The structure of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 7onv was solved by A.Stein, C.Dongping, Y.Cotelle, J.G.Rebelein, T.R.Ward, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.87 / 1.04
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.278, 71.807, 73.694, 90, 90, 90
R / Rfree (%) 18.3 / 20

Other elements in 7onv:

The structure of Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase) also contains other interesting chemical elements:

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

Iridium Binding Sites:

The binding sites of Iridium atom in the Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase) (pdb code 7onv). 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 Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 7onv:

Iridium binding site 1 out of 1 in 7onv

Go back to Iridium Binding Sites List in 7onv
Iridium binding site 1 out of 1 in the Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex 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 Carbonic Anhydrase II Mutant (I91C) Dually Binding An Ircp* Complex to Generate An Artificial Transfer Hydrogenase (Athase) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ir302

b:12.1
occ:1.00
 IR1 A:VKZ302 0.0 12.1 1.0
N2 A:VKZ302 2.1 12.6 1.0
N1 A:VKZ302 2.1 11.7 1.0
C13 A:VKZ302 2.1 12.0 1.0
C17 A:VKZ302 2.1 12.7 1.0
C16 A:VKZ302 2.2 14.1 1.0
C15 A:VKZ302 2.2 16.0 1.0
C14 A:VKZ302 2.2 13.4 1.0
CL1 A:VKZ302 2.4 33.7 1.0
C5 A:VKZ302 3.0 11.7 1.0
C6 A:VKZ302 3.0 12.3 1.0
C1 A:VKZ302 3.1 13.1 1.0
C23 A:VKZ302 3.2 12.0 1.0
C18 A:VKZ302 3.2 17.6 1.0
C19 A:VKZ302 3.3 16.1 1.0
C22 A:VKZ302 3.3 15.2 1.0
C20 A:VKZ302 3.4 15.5 1.0
C21 A:VKZ302 3.4 13.2 1.0
C24 A:VKZ302 4.1 13.2 1.0
O3 A:VKZ302 4.1 11.7 1.0
C2 A:VKZ302 4.4 12.3 1.0
C4 A:VKZ302 4.4 12.4 1.0
CE1 A:PHE130 4.5 10.5 1.0
CD1 A:PHE130 4.8 11.4 1.0
C3 A:VKZ302 4.9 12.9 1.0

Reference:

A.Stein, D.Chen, N.V.Igareta, Y.Cotelle, J.G.Rebelein, T.R.Ward. A Dual Anchoring Strategy For the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase. Acs Cent.Sci. V. 7 1874 2021.
ISSN: ESSN 2374-7951
PubMed: 34849402
DOI: 10.1021/ACSCENTSCI.1C00825
Page generated: Mon Aug 12 03:52:27 2024

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