Chlorine in PDB 4ulx: Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant.

Enzymatic activity of Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant.

All present enzymatic activity of Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant.:
4.7.1.4;

Protein crystallography data

The structure of Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant., PDB code: 4ulx was solved by J.A.Gavira, V.A.Risso, B.Ibarra-Molero, J.M.Sanchez-Ruiz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	32.794 / 2.35
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	35.172, 38.882, 61.040, 90.00, 90.00, 90.00
*R / R_free (%)*	19.92 / 24.37

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant. (pdb code 4ulx). 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 Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant., PDB code: 4ulx:

Chlorine binding site 1 out of 1 in 4ulx

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Chlorine Binding Sites List in 4ulx

Chlorine binding site 1 out of 1 in the Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant.

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Ancestral Thioredoxin, Relative to the Last Common Ancestor of the Cyanobacterial, Deinococcus and Thermus Groups, Lpbca-L89K Mutant. within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1107 b:48.4 occ:1.00	O	A:HOH2013	3.2	44.7	1.0
	NZ	A:LYS56	3.3	30.3	1.0
	CE3	A:TRP27	3.6	25.4	1.0
	O	A:CYS34	3.7	22.5	1.0
	CB	A:ALA38	3.7	26.9	1.0
	CD2	A:TRP27	3.9	24.1	1.0
	CE	A:LYS56	3.9	29.4	1.0
	C	A:CYS34	4.0	28.4	1.0
	CZ3	A:TRP27	4.1	27.0	1.0
	CG	A:TRP27	4.3	23.5	1.0
	CB	A:CYS34	4.3	22.1	1.0
	N	A:ARG35	4.4	29.1	1.0
	CB	A:TRP27	4.5	23.4	1.0
	CA	A:ARG35	4.5	32.9	1.0
	CE2	A:TRP27	4.6	21.9	1.0
	CA	A:CYS34	4.8	27.6	1.0
	CH2	A:TRP27	4.8	27.0	1.0
	CA	A:ALA38	4.8	26.5	1.0

Reference:

V.A.Risso, F.Manssour-Triedo, A.Delgado-Delgado, R.Arco, A.Barroso-Deljesus, A.Ingles-Prieto, R.Godoy-Ruiz, J.A.Gavira, E.A.Gaucher, B.Ibarra-Molero, J.M.Sanchez-Ruiz. Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific Amino Acid Preferences Throughout Evolutionary History. Mol.Biol.Evol. 2014.
ISSN: ESSN 1537-1719
PubMed: 25392342
DOI: 10.1093/MOLBEV/MSU312

Page generated: Sat Dec 12 11:15:48 2020

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