Chlorine in PDB 2iv0: Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers

Enzymatic activity of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers

All present enzymatic activity of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers:
1.1.1.42;

Protein crystallography data

The structure of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers, PDB code: 2iv0 was solved by R.Stokke, M.Karlstrom, N.Yang, I.Leiros, R.Ladenstein, N.K.Birkeland, I.H.Steen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	86.71 / 2.5
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	81.611, 65.405, 87.181, 90.00, 95.28, 90.00
*R / R_free (%)*	19.6 / 25.4

Other elements in 2iv0:

The structure of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers also contains other interesting chemical elements:

Zinc

(Zn)

9 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers (pdb code 2iv0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers, PDB code: 2iv0:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 2iv0

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Chlorine Binding Sites List in 2iv0

Chlorine binding site 1 out of 3 in the Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1417 b:14.9 occ:1.00	O	A:HOH2015	3.7	12.1	1.0
	ND2	A:ASN78	3.8	12.3	1.0
	OD2	A:ASP82	3.9	21.7	1.0
	N	A:ASP82	3.9	12.4	1.0
	CG	A:ASP82	4.1	16.4	1.0
	OE2	A:GLU4	4.3	18.0	1.0
	CA	A:PRO81	4.4	11.3	1.0
	CB	A:ASP82	4.4	13.6	1.0
	CB	A:ASN78	4.4	13.5	1.0
	CB	A:PRO81	4.5	10.8	1.0
	CG	A:ASN78	4.6	13.5	1.0
	CD2	A:TYR76	4.7	9.6	1.0
	C	A:PRO81	4.7	11.3	1.0
	OD1	A:ASP82	4.7	15.6	1.0
	CA	A:ASP82	4.8	13.5	1.0
	OE1	A:GLU4	4.9	22.7	1.0
	CD	A:GLU4	4.9	19.5	1.0

Chlorine binding site 2 out of 3 in 2iv0

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Chlorine Binding Sites List in 2iv0

Chlorine binding site 2 out of 3 in the Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1418 b:20.5 occ:1.00	ZN	A:ZN1415	2.8	15.1	1.0
	OD2	B:ASP277	3.5	15.5	1.0
	OD2	A:ASP305	4.0	22.5	1.0
	OD1	A:ASP301	4.5	18.4	1.0
	CD2	A:LEU314	4.6	21.0	1.0
	CG	B:ASP277	4.6	14.6	1.0
	OD1	A:ASP305	4.7	16.6	1.0
	NH2	A:ARG125	4.7	30.0	1.0
	CG	A:ASP305	4.8	16.4	1.0
	CG1	A:VAL332	5.0	21.5	1.0

Chlorine binding site 3 out of 3 in 2iv0

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Chlorine Binding Sites List in 2iv0

Chlorine binding site 3 out of 3 in the Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Cl1418 b:20.9 occ:1.00	O	B:HOH2023	2.3	4.7	1.0
	ZN	B:ZN1414	2.7	10.7	1.0
	OD2	A:ASP277	3.5	14.4	1.0
	O	A:HOH2040	3.7	17.3	1.0
	OD2	B:ASP305	3.8	9.2	1.0
	OH	B:TYR107	4.2	50.0	1.0
	OD1	B:ASP301	4.2	15.3	1.0
	CG1	B:VAL332	4.6	27.0	1.0
	CG	B:ASP305	4.7	10.0	1.0
	OD1	B:ASP305	4.7	10.9	1.0
	CG	A:ASP277	4.7	13.3	1.0

Reference:

R.Stokke, M.Karlstrom, N.Yang, I.Leiros, R.Ladenstein, N.K.Birkeland, I.H.Steen. Thermal Stability of Isocitrate Dehydrogenase From Archaeoglobus Fulgidus Studied By Crystal Structure Analysis and Engineering of Chimers Extremophiles V. 11 481 2007.
ISSN: ISSN 1431-0651
PubMed: 17401542
DOI: 10.1007/S00792-006-0060-Z

Page generated: Sat Jul 20 08:24:37 2024

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