Calcium in PDB 2eu8: Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R)

Enzymatic activity of Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R)

All present enzymatic activity of Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R):
2.7.4.3;

Protein crystallography data

The structure of Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R), PDB code: 2eu8 was solved by S.Chen, Y.Shamoo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	37.57 / 1.80
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	34.690, 75.140, 77.350, 90.00, 98.13, 90.00
*R / R_free (%)*	18.7 / 22.4

Other elements in 2eu8:

The structure of Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R) also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Zinc	(Zn)	2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R) (pdb code 2eu8). 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 Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R), PDB code: 2eu8:

Calcium binding site 1 out of 1 in 2eu8

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Calcium Binding Sites List in 2eu8

Calcium binding site 1 out of 1 in the Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R)

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Thermostable Mutant of Bacillus Subtilis Adenylate Kinase (Q199R) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:Ca1223 b:16.9 occ:1.00	O	B:ALA161	2.6	17.0	1.0
	OD1	B:ASN164	2.6	17.0	1.0
	O	A:GLY190	2.6	13.7	1.0
	O	B:HOH1245	2.7	12.7	1.0
	O	A:HOH1281	2.7	23.6	1.0
	O	A:HOH1302	2.7	22.9	1.0
	O	B:HOH1256	2.8	20.4	1.0
	CG	B:ASN164	3.4	17.4	1.0
	C	B:ALA161	3.6	15.4	1.0
	O	B:HOH1444	3.8	31.7	1.0
	C	A:GLY190	3.8	13.2	1.0
	ND2	B:ASN164	4.2	16.4	1.0
	CB	B:ASN164	4.2	18.6	1.0
	CA	A:TYR191	4.2	12.2	1.0
	CA	B:ALA161	4.3	15.3	1.0
	N	B:ASP162	4.4	13.3	1.0
	OG1	B:THR167	4.5	15.8	1.0
	CA	B:ASP162	4.5	12.6	1.0
	N	A:TYR191	4.5	13.1	1.0
	CB	B:ALA161	4.6	15.1	1.0
	O	A:HOH1362	4.8	16.6	1.0
	CB	A:TYR191	4.8	12.5	1.0
	O	A:HOH1247	4.8	15.6	1.0
	CE1	A:TYR109	4.8	18.9	1.0
	O	B:HOH1302	4.8	22.6	1.0
	O	B:ASP54	4.8	10.6	1.0
	CA	A:GLY190	4.9	13.7	1.0
	N	B:ASN164	4.9	16.2	1.0

Reference:

R.Counago, S.Chen, Y.Shamoo. In Vivo Molecular Evolution Reveals Biophysical Origins of Organismal Fitness. Mol.Cell V. 22 441 2006.
ISSN: ISSN 1097-2765
PubMed: 16713575
DOI: 10.1016/J.MOLCEL.2006.04.012

Page generated: Fri Jul 12 10:17:52 2024

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