Chlorine in PDB 4mu0: The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution

Enzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution

All present enzymatic activity of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution:
4.2.1.19;

Protein crystallography data

The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution, PDB code: 4mu0 was solved by C.Bisson, K.L.Britton, S.E.Sedelnikova, P.J.Baker, D.W.Rice, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	50.59 / 1.30
*Space group*	P 4 3 2
*Cell size a, b, c (Å), α, β, γ (°)*	113.130, 113.130, 113.130, 90.00, 90.00, 90.00
*R / R_free (%)*	13 / 14.8

Other elements in 4mu0:

The structure of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution also contains other interesting chemical elements:

Manganese

(Mn)

2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution (pdb code 4mu0). 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 The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution, PDB code: 4mu0:

Chlorine binding site 1 out of 1 in 4mu0

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Chlorine Binding Sites List in 4mu0

Chlorine binding site 1 out of 1 in the The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of The Structure of Wt A. Thaliana IGPD2 in Complex with MN2+ and 1,2,4- Triazole at 1.3 A Resolution within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl305 b:13.4 occ:0.33	NH1	A:ARG161	3.1	14.2	0.5
	NH2	A:ARG161	3.3	11.9	0.5
	NH2	A:ARG161	3.5	18.1	0.5
	NH1	A:ARG161	3.5	8.0	0.5
	CZ	A:ARG161	3.8	12.6	0.5
	CZ	A:ARG161	3.9	7.9	0.5
	C2	A:TRS304	4.1	12.9	0.3
	C1	A:TRS304	4.1	13.4	0.3
	C3	A:TRS304	4.1	11.9	0.3
	C	A:TRS304	4.4	12.3	0.3
	CD2	A:LEU163	4.4	13.8	1.0
	O3	A:TRS304	4.8	8.9	0.3
	CD1	A:LEU163	4.9	11.8	1.0

Reference:

C.Bisson, K.L.Britton, S.E.Sedelnikova, H.F.Rodgers, T.C.Eadsforth, R.Viner, T.R.Hawkes, P.J.Baker, D.W.Rice. A New Role For Metal Ions in Enzyme Catalysis To Be Published.

Page generated: Fri Jul 11 19:18:00 2025

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