Arsenic in PDB 4uhf: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound)

Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound)

All present enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound):
3.1.1.1;

Protein crystallography data

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound), PDB code: 4uhf 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)*	37.97 / 1.08
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.230, 43.230, 227.830, 90.00, 90.00, 120.00
*R / R_free (%)*	11.351 / 13.561

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound) (pdb code 4uhf). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound), PDB code: 4uhf:

Arsenic binding site 1 out of 1 in 4uhf

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Arsenic Binding Sites List in 4uhf

Arsenic binding site 1 out of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound)

Mono view

Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (L37A Mutant with Butyrate Bound) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:As1280 b:12.0 occ:0.70	AS	A:CAD1280	0.0	12.0	0.7
	O1	A:CAD1280	1.6	9.7	0.7
	O2	A:CAD1280	1.7	14.5	0.7
	C2	A:CAD1280	1.9	11.9	0.7
	C1	A:CAD1280	1.9	13.5	0.7
	O	A:HOH2318	3.7	35.1	1.0
	OH	A:TYR105	3.7	10.3	1.0
	O	A:HOH2319	3.8	47.2	1.0
	NH2	A:ARG139	3.8	11.1	1.0
	NH1	A:ARG139	3.8	11.3	1.0
	O	A:HOH2126	3.9	15.8	0.6
	OG	A:SER101	4.1	11.2	0.8
	O	A:HOH2317	4.2	38.3	1.0
	CZ	A:ARG139	4.3	9.9	1.0
	NH1	A:ARG127	4.3	30.4	0.3
	O	A:HOH2124	4.3	16.1	1.0
	O1	A:BUA1281	4.3	12.0	0.8
	CE2	A:TYR105	4.5	7.5	1.0
	CZ	A:TYR105	4.5	8.0	1.0
	O	A:HOH2320	4.7	15.8	0.7
	SD	A:MET197	4.7	9.8	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: Wed Jul 10 12:29:02 2024

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