Magnesium in PDB 3gup: T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding

Enzymatic activity of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding

All present enzymatic activity of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding:
3.2.1.17;

Protein crystallography data

The structure of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding, PDB code: 3gup was solved by L.Liu, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	48.96 / 1.50
*Space group*	P 4₃
*Cell size a, b, c (Å), α, β, γ (°)*	48.957, 48.957, 129.315, 90.00, 90.00, 90.00
*R / R_free (%)*	21.1 / 25.3

Other elements in 3gup:

The structure of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding (pdb code 3gup). 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 T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding, PDB code: 3gup:

Magnesium binding site 1 out of 1 in 3gup

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Magnesium Binding Sites List in 3gup

Magnesium binding site 1 out of 1 in the T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding

Mono view

Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity-- Pyridine Binding within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Mg166 b:23.3 occ:1.00	OH	A:TYR88	3.0	24.3	1.0
	OH	B:TYR88	3.1	23.4	1.0
	NH1	B:ARG96	3.3	23.0	1.0
	NH1	A:ARG96	3.3	23.1	1.0
	CE2	A:TYR88	3.6	24.0	1.0
	CE2	B:TYR88	3.6	24.0	1.0
	CZ	B:TYR88	3.8	22.4	1.0
	CZ	A:TYR88	3.9	21.6	1.0
	N1	A:0PY169	4.1	39.9	1.0
	CD	B:ARG96	4.1	25.1	1.0
	CD	A:ARG96	4.1	24.8	1.0
	CZ	B:ARG96	4.4	23.1	1.0
	CZ	A:ARG96	4.5	23.0	1.0
	CZ	B:CME97	4.7	26.8	1.0
	CZ	A:CME97	4.7	26.8	1.0
	NE	B:ARG96	4.7	23.5	1.0
	NE	A:ARG96	4.8	22.4	1.0
	C5	A:0PY169	4.8	38.7	1.0
	C1	A:0PY169	4.9	40.0	1.0
	CD2	A:TYR88	4.9	23.0	1.0
	CD2	B:TYR88	4.9	22.7	1.0
	CE	A:CME97	5.0	25.9	1.0

Reference:

L.Liu, W.A.Baase, M.M.Michael, B.W.Matthews. Use of Stabilizing Mutations to Engineer A Charged Group Within A Ligand-Binding Hydrophobic Cavity in T4 Lysozyme. Biochemistry V. 48 8842 2009.
ISSN: ISSN 0006-2960
PubMed: 19663503
DOI: 10.1021/BI900685J

Page generated: Wed Aug 14 14:57:28 2024

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