Magnesium in PDB 4uhd: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)

Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)

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

Protein crystallography data

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound), PDB code: 4uhd 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)*	37.48 / 1.07
*Space group*	P 3₂ 2 1
*Cell size a, b, c (Å), α, β, γ (°)*	43.280, 43.280, 227.290, 90.00, 90.00, 120.00
*R / R_free (%)*	9.351 / 11.203

Other elements in 4uhd:

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

Chlorine

(Cl)

1 atom

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 1 in 4uhd

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Magnesium Binding Sites List in 4uhd

Magnesium binding site 1 out of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg1277 b:12.6 occ:1.00	O	A:ILE237	2.3	11.0	1.0
	OG	A:SER240	2.3	11.3	1.0
	O	A:HOH2317	2.3	16.2	1.0
	O	A:HOH2316	2.4	20.1	1.0
	O	A:ALA234	2.4	11.8	1.0
	O	A:HOH2326	2.6	14.0	1.0
	CB	A:SER240	3.4	11.0	1.0
	C	A:ILE237	3.4	8.9	1.0
	C	A:ALA234	3.6	10.9	1.0
	N	A:ILE237	3.9	8.5	1.0
	CA	A:ARG235	4.1	13.1	0.3
	CA	A:ARG235	4.1	12.1	0.3
	CA	A:ARG235	4.1	11.4	0.3
	C	A:ARG235	4.1	10.8	1.0
	N	A:SER240	4.2	9.8	1.0
	CA	A:ILE237	4.2	8.4	1.0
	O	A:HOH2320	4.3	18.9	1.0
	N	A:ARG235	4.3	12.1	1.0
	O	A:ARG235	4.3	11.7	1.0
	CA	A:SER240	4.4	9.6	1.0
	C	A:PRO238	4.4	9.4	0.4
	N	A:PRO238	4.4	8.4	0.4
	O	A:PRO238	4.4	10.7	0.4
	N	A:PRO238	4.4	8.2	0.6
	CA	A:PRO238	4.5	10.1	0.4
	O	A:HOH2318	4.5	28.0	1.0
	CB	A:ILE237	4.5	9.8	1.0
	N	A:THR236	4.6	11.5	1.0
	CA	A:PRO238	4.6	9.0	0.6
	NH1	A:ARG235	4.6	21.9	0.3
	CA	A:ALA234	4.7	11.2	1.0
	C	A:PRO238	4.8	8.0	0.6
	C	A:THR236	4.8	8.6	1.0
	N	A:GLN239	4.9	10.2	0.4
	O	A:SER240	4.9	10.9	1.0
	N	A:GLN239	5.0	8.5	0.6
	CB	A:ALA234	5.0	12.3	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: Tue Aug 20 04:43:14 2024

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