Sodium 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
Manganese	(Mn)	2 atoms
Calcium	(Ca)	1 atom

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

Sodium 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 Sodium with other atoms in the Na 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:Na1201 b:9.5 occ:1.00 O A:GLY256 2.4 9.7 1.0 O A:TRP234 2.4 8.6 1.0 OD1 A:ASP233 2.4 10.2 1.0 O A:LYS253 2.5 9.0 1.0 OG1 A:THR257 2.7 10.6 1.0 N A:TRP234 3.2 9.3 1.0 C A:GLY256 3.4 8.8 1.0 C A:TRP234 3.4 9.4 1.0 C A:ASP233 3.4 8.4 1.0 C A:LYS253 3.5 9.2 1.0 CG A:ASP233 3.6 9.6 1.0 CA A:ASP233 3.7 9.2 1.0 CA A:TRP234 3.8 9.2 1.0 CA A:LYS253 3.8 8.9 1.0 CB A:THR257 3.8 8.8 1.0 CA A:THR257 3.9 8.1 1.0 O A:ASP233 4.0 9.3 1.0 N A:THR257 4.0 8.5 1.0 O A:HOH1296 4.1 10.1 1.0 CB A:LYS253 4.2 9.2 1.0 CB A:TRP234 4.2 9.9 1.0 CB A:ASP233 4.3 9.2 1.0 N A:GLY256 4.5 10.1 1.0 CG2 A:THR257 4.5 9.6 1.0 CA A:GLY256 4.5 9.1 1.0 CD A:LYS253 4.6 10.7 1.0 O A:HOH1499 4.6 10.8 1.0 OD2 A:ASP233 4.6 9.6 1.0 N A:SER235 4.6 8.8 1.0 N A:SER254 4.7 8.5 1.0 O A:HOH1298 4.7 9.9 1.0 O A:ASN232 4.9 8.8 1.0 CD1 A:TRP234 5.0 7.8 1.0

Sodium 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 Sodium with other atoms in the Na 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:Na1202 b:9.8 occ:1.00 O B:GLY256 2.4 9.5 1.0 OD1 B:ASP233 2.4 11.0 1.0 O B:TRP234 2.4 9.5 1.0 O B:LYS253 2.5 10.5 1.0 OG1 B:THR257 2.7 10.4 1.0 N B:TRP234 3.2 9.2 1.0 C B:GLY256 3.4 9.7 1.0 C B:ASP233 3.4 8.6 1.0 C B:TRP234 3.4 9.7 1.0 C B:LYS253 3.5 9.5 1.0 CG B:ASP233 3.6 11.2 1.0 CA B:ASP233 3.7 9.5 1.0 CA B:TRP234 3.8 10.1 1.0 CA B:LYS253 3.8 10.1 1.0 CB B:THR257 3.9 9.0 1.0 CA B:THR257 4.0 9.1 1.0 O B:ASP233 4.0 9.3 1.0 O B:HOH1550 4.0 10.3 1.0 N B:THR257 4.1 9.3 1.0 CB B:LYS253 4.1 9.9 1.0 CB B:TRP234 4.2 9.6 1.0 CB B:ASP233 4.3 10.6 1.0 N B:GLY256 4.4 9.7 1.0 CG2 B:THR257 4.5 11.3 1.0 CD B:LYS253 4.5 10.9 1.0 CA B:GLY256 4.5 10.4 1.0 OD2 B:ASP233 4.6 10.2 1.0 O B:HOH1288 4.6 10.9 1.0 N B:SER235 4.6 9.7 1.0 N B:SER254 4.7 8.9 1.0 O B:HOH1279 4.7 9.5 1.0 O B:ASN232 4.9 9.0 1.0 CD1 B:TRP234 5.0 9.2 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