Manganese in PDB 2hzy: 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;

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

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
Calcium	(Ca)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Manganese 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 Manganese atom.
In total 2 binding sites of Manganese where determined in the Mouse Fumarylacetoacetate Hydrolase Complexes with A Transition-State Mimic of the Complete Substrate, PDB code: 2hzy:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 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 Manganese with other atoms in the Mn 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:Mn1203 b:9.1 occ:1.00 O1 A:DHJ1102 2.1 11.0 1.0 OE2 A:GLU201 2.1 9.8 1.0 OE2 A:GLU199 2.1 12.2 1.0 OD2 A:ASP233 2.1 9.6 1.0 OD2 A:ASP126 2.1 10.8 1.0 O5 A:DHJ1102 2.2 10.9 1.0 C2 A:DHJ1102 3.1 10.1 1.0 C5 A:DHJ1102 3.1 9.4 1.0 CG A:ASP233 3.1 9.6 1.0 CD A:GLU201 3.2 9.5 1.0 CG A:ASP126 3.2 9.2 1.0 CD A:GLU199 3.3 14.8 1.0 C4 A:DHJ1102 3.4 10.2 1.0 CB A:ASP233 3.4 9.2 1.0 OD1 A:ASP126 3.6 9.7 1.0 OE1 A:GLU201 3.7 9.2 1.0 OE1 A:GLU199 3.8 16.5 1.0 NZ A:LYS253 3.8 16.5 1.0 OH A:TYR159 3.9 9.9 1.0 OG1 A:THR350 4.0 11.3 1.0 O3 A:DHJ1102 4.2 10.7 1.0 OD1 A:ASP233 4.3 10.2 1.0 CG A:GLU201 4.4 8.9 1.0 CG A:GLU199 4.5 13.2 1.0 CB A:GLU199 4.5 10.7 1.0 CE A:LYS253 4.5 12.4 1.0 CB A:ASP126 4.5 9.3 1.0 C6 A:DHJ1102 4.5 12.3 1.0 N A:THR350 4.8 9.1 1.0 CZ A:TYR159 4.9 9.3 1.0 CE2 A:TYR159 4.9 9.8 1.0 CA A:ASP233 5.0 9.2 1.0 O A:HOH1296 5.0 10.1 1.0

Manganese binding site 2 out of 2 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 Manganese with other atoms in the Mn binding site number 2 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 B:Mn1204 b:9.0 occ:1.00 OE2 B:GLU201 2.1 9.2 1.0 O1 B:DHJ1101 2.1 10.8 1.0 OE1 B:GLU199 2.1 11.4 1.0 OD2 B:ASP233 2.2 10.2 1.0 OD2 B:ASP126 2.2 9.3 1.0 O5 B:DHJ1101 2.2 10.4 1.0 C2 B:DHJ1101 3.1 11.3 1.0 CG B:ASP233 3.1 11.2 1.0 C5 B:DHJ1101 3.1 10.2 1.0 CD B:GLU201 3.2 9.9 1.0 CG B:ASP126 3.2 7.6 1.0 CD B:GLU199 3.3 11.2 1.0 CB B:ASP233 3.4 10.6 1.0 C4 B:DHJ1101 3.4 11.5 1.0 OD1 B:ASP126 3.6 10.0 1.0 OE1 B:GLU201 3.7 8.9 1.0 NZ B:LYS253 3.8 12.6 1.0 OE2 B:GLU199 3.9 13.4 1.0 OH B:TYR159 3.9 10.1 1.0 OG1 B:THR350 4.1 11.2 1.0 O3 B:DHJ1101 4.2 10.6 1.0 OD1 B:ASP233 4.3 11.0 1.0 CG B:GLU201 4.4 9.1 1.0 CB B:GLU199 4.4 10.8 1.0 CG B:GLU199 4.5 12.5 1.0 C6 B:DHJ1101 4.5 10.8 1.0 CB B:ASP126 4.6 9.1 1.0 CE B:LYS253 4.6 10.2 1.0 N B:THR350 4.8 10.0 1.0 CA B:ASP233 4.9 9.5 1.0 O7 B:DHJ1101 4.9 14.2 1.0 CD B:LYS253 4.9 10.9 1.0 CZ B:TYR159 5.0 8.5 1.0 CE2 B:TYR159 5.0 9.3 1.0 O B:HOH1550 5.0 10.3 1.0

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