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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 / Rfree (%) 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

Go back to 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: Sat Dec 12 03:53:18 2020

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