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Calcium in PDB 2jfp: Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate

Enzymatic activity of Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate

All present enzymatic activity of Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate:
5.1.1.3;

Protein crystallography data

The structure of Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate, PDB code: 2jfp was solved by T.Lundqvist, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.00 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.190, 74.670, 75.070, 90.00, 95.97, 90.00
R / Rfree (%) n/a / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate (pdb code 2jfp). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate, PDB code: 2jfp:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2jfp

Go back to Calcium Binding Sites List in 2jfp
Calcium binding site 1 out of 2 in the Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate


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 Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1271

b:22.3
occ:1.00
O A:HOH2242 2.9 12.6 1.0
O A:HOH2050 2.9 16.5 1.0
N A:LEU119 3.2 13.7 1.0
CB A:THR118 3.6 13.4 1.0
CG A:LEU119 3.6 15.5 1.0
CA A:GLY44 3.6 15.2 1.0
CA A:PRO146 3.7 14.4 1.0
CA A:THR118 3.7 13.1 1.0
C A:GLY44 3.8 15.4 1.0
CB A:PRO146 3.8 14.5 1.0
CD1 A:LEU119 3.9 16.4 1.0
CB A:LEU119 3.9 14.7 1.0
C A:THR118 4.0 13.4 1.0
O A:HOH2133 4.0 16.6 1.0
N A:PRO45 4.1 15.2 1.0
CD A:PRO45 4.1 15.6 1.0
CA A:LEU119 4.2 13.7 1.0
CG2 A:THR118 4.2 13.6 1.0
O A:GLY44 4.2 14.8 1.0
N A:PRO146 4.3 13.9 1.0
O A:HOH2132 4.4 11.5 1.0
C A:PRO146 4.7 15.0 1.0
O A:PRO146 4.8 14.9 1.0
N A:GLY44 4.8 14.7 1.0
CD A:PRO146 4.8 13.9 1.0
OG1 A:THR118 4.9 13.0 1.0
CA A:PRO45 4.9 15.9 1.0
OE1 A:DGL1270 4.9 21.0 1.0
CB A:PRO45 4.9 16.6 1.0
C A:CYS145 5.0 12.6 1.0
CG A:PRO146 5.0 14.0 1.0
CD2 A:LEU119 5.0 17.3 1.0

Calcium binding site 2 out of 2 in 2jfp

Go back to Calcium Binding Sites List in 2jfp
Calcium binding site 2 out of 2 in the Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Enterococcus Faecalis Glutamate Racemase in Complex with D- Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1271

b:21.5
occ:1.00
O B:HOH2068 3.0 25.0 1.0
O B:HOH2261 3.1 9.9 1.0
N B:LEU119 3.2 10.3 1.0
CG B:LEU119 3.5 12.8 1.0
CD1 B:LEU119 3.6 14.8 1.0
CA B:GLY44 3.6 11.9 1.0
CB B:THR118 3.7 9.8 1.0
C B:GLY44 3.7 12.7 1.0
CA B:THR118 3.7 10.5 1.0
CA B:PRO146 3.8 13.3 1.0
CB B:LEU119 3.8 12.2 1.0
O B:HOH2160 3.9 18.9 1.0
N B:PRO45 3.9 12.6 1.0
CB B:PRO146 3.9 14.3 1.0
C B:THR118 4.0 10.3 1.0
CD B:PRO45 4.0 12.4 1.0
O B:GLY44 4.1 12.0 1.0
CA B:LEU119 4.1 10.6 1.0
CG2 B:THR118 4.1 10.0 1.0
N B:PRO146 4.4 12.9 1.0
O B:HOH2159 4.4 13.4 1.0
CA B:PRO45 4.7 13.5 1.0
CB B:PRO45 4.7 13.3 1.0
N B:GLY44 4.7 12.8 1.0
O B:PRO146 4.8 13.2 1.0
C B:PRO146 4.8 13.2 1.0
OG1 B:THR118 4.9 10.0 1.0
CG B:PRO45 4.9 13.4 1.0
CD2 B:LEU119 4.9 14.5 1.0
N B:GLY120 5.0 9.8 1.0
OE1 B:DGL1270 5.0 19.9 1.0
CD B:PRO146 5.0 13.0 1.0

Reference:

T.Lundqvist, S.L.Fisher, G.Kern, R.H.A.Folmer, Y.Xue, D.T.Newton, T.A.Keating, R.A.Alm, B.L.M.De Jonge. Exploitation of Structural and Regulatory Diversity in Glutamate Racemases Nature V. 447 817 2007.
ISSN: ISSN 0028-0836
PubMed: 17568739
DOI: 10.1038/NATURE05689
Page generated: Sat Dec 12 03:42:07 2020

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