Chlorine 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 / R_free (%)*	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:

Zinc	(Zn)	1 atom
Iridium	(Ir)	1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Human Carbonic Anhydrase II with Bound Ircp* Complex (Cofactor 10) to Generate An Artificial Transfer Hydrogenase (Athase), PDB code: 6qfx:

Chlorine binding site 1 out of 1 in 6qfx

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Chlorine Binding Sites List in 6qfx

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl301 b:56.0 occ:0.60	CL1	A:JR3301	0.0	56.0	0.6
	IR1	A:JR3301	2.5	41.9	0.6
	N2	A:JR3301	2.5	44.1	1.0
	C14	A:JR3301	3.0	42.7	0.6
	C21	A:JR3301	3.1	40.6	0.6
	N1	A:JR3301	3.1	40.6	1.0
	C6	A:JR3301	3.1	46.0	1.0
	C13	A:JR3301	3.2	42.4	0.6
	C23	A:JR3301	3.4	46.3	1.0
	C5	A:JR3301	3.4	44.1	1.0
	C22	A:JR3301	3.5	40.3	0.6
	C15	A:JR3301	3.8	42.3	0.6
	O3	A:JR3301	4.0	47.2	1.0
	C1	A:JR3301	4.0	47.2	1.0
	C17	A:JR3301	4.1	41.2	0.6
	C16	A:JR3301	4.4	42.9	0.6
	C20	A:JR3301	4.7	42.5	0.6
	C4	A:JR3301	4.7	46.9	1.0
	C24	A:JR3301	4.7	49.0	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: Mon Jul 29 13:56:34 2024

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