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Calcium in PDB 2hzy: Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate

Enzymatic activity of Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate

All present enzymatic activity of Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate:
3.7.1.2;

Protein crystallography data

The structure of Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate, PDB code: 2hzy was solved by T.D.Hurley, D.E.Timm, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.14 / 1.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 64.144, 109.472, 67.491, 90.00, 102.35, 90.00
R / Rfree (%) 16.8 / 18.8

Other elements in 2hzy:

The structure of Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate also contains other interesting chemical elements:

Nickel (Ni) 10 atoms
Manganese (Mn) 2 atoms
Sodium (Na) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate (pdb code 2hzy). 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 Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate, PDB code: 2hzy:

Calcium binding site 1 out of 1 in 2hzy

Go back to Calcium Binding Sites List in 2hzy
Calcium binding site 1 out of 1 in the Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca1206

b:10.7
occ:1.00
 O A:GLY122 2.7 10.4 1.0
O B:GLY122 2.7 10.7 1.0
O B:HOH1274 2.8 9.9 1.0
O A:HOH1343 2.8 8.9 1.0
OD1 A:ASP123 2.8 9.5 1.0
OD1 B:ASP123 2.8 8.2 1.0
CG A:ASP123 3.7 10.3 1.0
CG B:ASP123 3.7 9.4 1.0
CA B:ASP123 3.7 8.7 1.0
CA A:ASP123 3.7 9.4 1.0
C B:GLY122 3.8 9.5 1.0
C A:GLY122 3.8 10.3 1.0
CB B:ALA163 3.8 9.1 1.0
CB A:ALA163 3.9 10.7 1.0
O A:HOH1345 3.9 10.5 1.0
O B:HOH1548 3.9 9.8 1.0
N B:ASP123 4.2 9.0 1.0
N A:ASP123 4.2 10.4 1.0
CB B:ASP123 4.2 9.7 1.0
CB A:ASP123 4.3 9.8 1.0
O A:HOH1353 4.4 14.3 1.0
O B:HOH1292 4.4 14.0 1.0
OD2 A:ASP123 4.5 10.7 1.0
OD2 B:ASP123 4.5 10.6 1.0
N A:ALA163 4.6 8.3 1.0
N B:ALA163 4.7 8.8 1.0
N B:TYR124 4.7 7.6 1.0
N A:TYR124 4.7 9.0 1.0
C B:ASP123 4.8 8.2 1.0
C A:ASP123 4.8 9.2 1.0
CA B:ALA163 4.9 8.9 1.0
CA A:ALA163 4.9 9.2 1.0
O A:GLY161 5.0 8.3 1.0

Reference:

R.L.Bateman, J.Ashworth, J.F.Witte, L.J.Baker, P.Bhanumoorthy, D.E.Timm, T.D.Hurley, M.Grompe, R.W.Mcclard. Slow-Onset Inhibition of Fumarylacetoacetate Hydrolase By Phosphinate Mimics of the Tetrahedral Intermediate: Kinetics, Crystal Structure and Pharmacokinetics. Biochem.J. V. 402 251 2007.
ISSN: ISSN 0264-6021
PubMed: 17064256
DOI: 10.1042/BJ20060961
Page generated: Fri Jul 12 12:53:14 2024

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