Calcium in PDB 2v9m: L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A)

Enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A)

All present enzymatic activity of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A):
4.1.2.19;

Protein crystallography data

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A), PDB code: 2v9m was solved by D.Grueninger, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	20.00 / 1.30
*Space group*	P 4
*Cell size a, b, c (Å), α, β, γ (°)*	83.407, 83.407, 97.299, 90.00, 90.00, 90.00
*R / R_free (%)*	10.4 / 14.1

Other elements in 2v9m:

The structure of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A) also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A) (pdb code 2v9m). 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 L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A), PDB code: 2v9m:

Calcium binding site 1 out of 1 in 2v9m

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Calcium Binding Sites List in 2v9m

Calcium binding site 1 out of 1 in the L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A)

Mono view

Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of L-Rhamnulose-1-Phosphate Aldolase From Escherichia Coli (Mutant A87M- T109F-E192A) within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Ca1276 b:13.0 occ:1.00	O3	A:CIT1278	2.0	27.7	1.0
	O	A:HOH2411	2.0	23.4	1.0
	NE2	A:HIS204	2.1	15.1	1.0
	O	A:HOH2324	2.1	19.8	1.0
	OE2	A:GLU200	2.2	17.9	1.0
	O	A:HOH2409	2.5	63.0	1.0
	CD2	A:HIS204	3.0	14.0	1.0
	C5	A:CIT1278	3.0	29.3	1.0
	CE1	A:HIS204	3.1	15.0	1.0
	CD	A:GLU200	3.2	19.8	1.0
	O4	A:CIT1278	3.3	38.8	1.0
	OE1	A:GLU200	3.4	30.2	1.0
	O	A:HOH2410	4.0	37.4	1.0
	OG1	A:THR158	4.1	14.2	1.0
	CG	A:HIS204	4.2	12.3	1.0
	ND1	A:HIS204	4.2	13.2	1.0
	CG2	A:THR158	4.2	13.3	1.0
	CA	A:GLY181	4.2	12.5	1.0
	O	A:HOH2319	4.2	35.9	1.0
	C4	A:CIT1278	4.4	28.4	1.0
	CG	A:GLU200	4.5	14.4	1.0
	CB	A:THR158	4.6	12.6	1.0
	O	A:HOH2323	4.6	51.7	1.0
	CB	A:LYS203	4.7	21.5	1.0
	CB	A:GLU200	4.9	12.7	1.0
	O5	A:CIT1278	4.9	31.9	1.0
	C2	A:CIT1278	5.0	27.4	1.0
	CA	A:GLU200	5.0	11.9	1.0

Reference:

D.Grueninger, N.Treiber, M.O.P.Ziegler, J.W.A.Koetter, M.-S.Schulze, G.E.Schulz. Designed Protein-Protein Association. Science V. 319 206 2008.
ISSN: ISSN 0036-8075
PubMed: 18187656
DOI: 10.1126/SCIENCE.1150421

Page generated: Fri Jul 12 17:51:58 2024

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