Calcium in PDB 3gum: T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity--P- Xylene Binding

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

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

Protein crystallography data

The structure of T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity--P- Xylene Binding, PDB code: 3gum 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)*	46.42 / 2.24
*Space group*	P 4₃
*Cell size a, b, c (Å), α, β, γ (°)*	49.709, 49.709, 129.710, 90.00, 90.00, 90.00
*R / R_free (%)*	21.8 / 26.4

Other elements in 3gum:

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

Chlorine

(Cl)

3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity--P- Xylene Binding (pdb code 3gum). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the T4 Lysozyme M102E/L99A Mutant with Buried Charge in Apolar Cavity--P- Xylene Binding, PDB code: 3gum:

Calcium binding site 1 out of 1 in 3gum

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Calcium Binding Sites List in 3gum

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

Mono view

Stereo pair view

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

probe	atom	residue	distance (Å)	B	Occ
B:Ca165 b:66.7 occ:1.00	OH	B:TYR88	3.2	36.2	1.0
	NH1	B:ARG96	3.3	30.9	1.0
	OH	A:TYR88	3.3	37.2	1.0
	NH1	A:ARG96	3.7	31.0	1.0
	CE2	B:TYR88	3.7	31.8	1.0
	CE2	A:TYR88	3.7	31.2	1.0
	CZ	B:TYR88	3.9	34.5	1.0
	CZ	A:TYR88	4.0	33.5	1.0
	CD	B:ARG96	4.2	34.9	1.0
	CZ	B:ARG96	4.4	35.0	1.0
	CD	A:ARG96	4.5	35.5	1.0
	NE	B:ARG96	4.7	33.9	1.0
	CZ	A:ARG96	4.8	35.9	1.0
	CD2	B:TYR88	4.9	33.1	1.0
	CD2	A:TYR88	5.0	33.5	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: Sat Jul 13 10:48:00 2024

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