Calcium in PDB 1qco: Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate

All present enzymatic activity of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate:
3.7.1.2;

The structure of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate, PDB code: 1qco was solved by D.E.Timm, H.A.Mueller, P.Bhanumoorthy, J.M.Harp, G.J.Bunick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.90 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.640, 110.940, 67.810, 90.00, 102.52, 90.00
R / Rfree (%)	15.9 / 19.2

The structure of Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate also contains other interesting chemical elements:

Nickel

(Ni)

5 atoms

The binding sites of Calcium atom in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate (pdb code 1qco). 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 Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate, PDB code: 1qco:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate


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 Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1002 b:10.5 occ:1.00 OD2 A:ASP126 2.3 10.6 1.0 OD2 A:ASP233 2.3 13.3 1.0 OE2 A:GLU201 2.4 11.2 1.0 OE1 A:GLU199 2.4 12.0 1.0 O3 A:AAE1010 2.4 14.3 1.0 O8 A:AAE1010 2.4 14.5 1.0 CG A:ASP233 3.3 11.4 1.0 C2 A:AAE1010 3.3 16.2 1.0 C5 A:AAE1010 3.4 17.2 1.0 CG A:ASP126 3.4 11.7 1.0 CD A:GLU201 3.4 12.6 1.0 CD A:GLU199 3.5 12.2 1.0 CB A:ASP233 3.6 9.0 1.0 C4 A:AAE1010 3.6 14.4 1.0 OD1 A:ASP126 3.7 11.5 1.0 NZ A:LYS253 3.8 16.5 1.0 OE1 A:GLU201 3.9 11.9 1.0 OH A:TYR159 4.0 14.9 1.0 OG1 A:THR350 4.1 12.7 1.0 OE2 A:GLU199 4.2 14.3 1.0 CE A:LYS253 4.4 15.0 1.0 OD1 A:ASP233 4.5 11.5 1.0 CB A:GLU199 4.5 11.3 1.0 O1 A:AAE1010 4.5 13.9 1.0 CG A:GLU199 4.6 12.4 1.0 CG A:GLU201 4.6 10.9 1.0 O A:HOH1255 4.6 16.7 1.0 CB A:ASP126 4.7 8.0 1.0 N A:THR350 4.7 12.9 1.0 C9 A:AAE1010 4.8 16.6 1.0 CA A:GLY349 5.0 12.6 1.0 CE2 A:TYR159 5.0 11.1 1.0 CZ A:TYR159 5.0 14.0 1.0 CD A:LYS253 5.0 16.1 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate


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 Fumarylacetoacetate Hydrolase Complexed with Fumarate and Acetoacetate within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca1001 b:12.8 occ:1.00 O8 B:AAE1011 2.3 11.9 1.0 OE2 B:GLU701 2.3 11.5 1.0 O3 B:AAE1011 2.3 15.5 1.0 OD2 B:ASP733 2.3 11.9 1.0 OE1 B:GLU699 2.4 16.5 1.0 OD2 B:ASP626 2.4 11.8 1.0 C5 B:AAE1011 3.3 13.4 1.0 C2 B:AAE1011 3.3 17.0 1.0 CG B:ASP733 3.3 14.1 1.0 CD B:GLU701 3.4 11.4 1.0 CG B:ASP626 3.4 14.1 1.0 CD B:GLU699 3.5 16.0 1.0 CB B:ASP733 3.6 10.0 1.0 C4 B:AAE1011 3.6 13.4 1.0 OD1 B:ASP626 3.8 12.8 1.0 NZ B:LYS753 3.9 16.1 1.0 OE1 B:GLU701 3.9 11.6 1.0 OH B:TYR659 4.0 10.5 1.0 OG1 B:THR850 4.1 14.5 1.0 OE2 B:GLU699 4.2 18.1 1.0 O1 B:AAE1011 4.4 14.9 1.0 OD1 B:ASP733 4.5 11.3 1.0 CB B:GLU699 4.5 12.0 1.0 CE B:LYS753 4.5 15.2 1.0 CG B:GLU701 4.6 10.6 1.0 O B:HOH1269 4.6 16.7 1.0 CG B:GLU699 4.6 14.2 1.0 C9 B:AAE1011 4.7 13.1 1.0 N B:THR850 4.7 14.1 1.0 CB B:ASP626 4.8 10.0 1.0 CZ B:TYR659 5.0 12.4 1.0 CE2 B:TYR659 5.0 11.8 1.0 CD B:LYS753 5.0 13.7 1.0

D.E.Timm, H.A.Mueller, P.Bhanumoorthy, J.M.Harp, G.J.Bunick. Crystal Structure and Mechanism of A Carbon-Carbon Bond Hydrolase. Structure Fold.Des. V. 7 1023 1999.
ISSN: ISSN 0969-2126
PubMed: 10508789
DOI: 10.1016/S0969-2126(99)80170-1