Chlorine in PDB 4uhh: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)

Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)

All present enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex):
3.1.1.1;

Protein crystallography data

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex), PDB code: 4uhh was solved by C.Sayer, M.N.Isupov, E.Bonch-Osmolovskaya, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	37.81 / 1.06
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.310, 43.310, 226.850, 90.00, 90.00, 120.00
*R / R_free (%)*	10.295 / 12.312

Other elements in 4uhh:

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex) also contains other interesting chemical elements:

Arsenic

(As)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex) (pdb code 4uhh). 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 Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex), PDB code: 4uhh:

Chlorine binding site 1 out of 1 in 4uhh

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Chlorine Binding Sites List in 4uhh

Chlorine binding site 1 out of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex)

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Cacodylate Complex) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl1277 b:12.9 occ:0.70	O	A:HOH2232	2.8	7.8	1.0
	O	A:HOH2208	2.8	13.6	1.0
	O	A:TYR105	2.9	6.1	1.0
	C	A:TYR105	3.6	5.6	1.0
	CB	A:MET75	3.7	7.1	1.0
	CG	A:MET75	3.8	7.6	1.0
	CB	A:TYR105	3.8	5.8	1.0
	CA	A:TYR105	3.9	5.6	1.0
	CD	A:ARG200	3.9	7.2	1.0
	CB	A:ARG200	3.9	7.4	1.0
	OG	A:SER203	4.2	10.6	1.0
	N	A:ALA109	4.2	6.6	1.0
	CG	A:ARG200	4.2	6.8	1.0
	CB	A:PHE108	4.3	7.2	1.0
	CB	A:ALA109	4.3	7.2	1.0
	CD	A:PRO201	4.4	10.4	1.0
	NH1	A:ARG112	4.4	17.6	0.4
	O	A:PRO201	4.6	9.2	1.0
	CA	A:ALA109	4.7	6.9	1.0
	O	A:HOH2056	4.8	13.2	1.0
	CG	A:PRO201	4.8	12.1	1.0
	N	A:VAL106	4.8	5.2	1.0
	O	A:HOH2225	4.8	8.1	1.0
	NE	A:ARG200	4.8	6.7	1.0
	CG	A:TYR105	4.8	5.8	1.0
	C	A:PHE108	4.9	6.8	1.0
	CA	A:ARG200	5.0	7.2	1.0

Reference:

C.Sayer, M.N.Isupov, E.Bonch-Osmolovskaya, J.A.Littlechild. Structural Studies of A Thermophilic Esterase From A New Planctomycetes Species, Thermogutta Terrifontis. Febs J. V. 282 2846 2015.
ISSN: ISSN 1742-464X
PubMed: 26011036
DOI: 10.1111/FEBS.13326

Page generated: Fri Jul 11 22:05:55 2025

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