Sodium in PDB 4z9o: Crystal Structure of Human GGT1

All present enzymatic activity of Crystal Structure of Human GGT1:
2.3.2.2; 3.4.19.13; 3.4.19.14;

The structure of Crystal Structure of Human GGT1, PDB code: 4z9o was solved by S.S.Terzyan, M.H.Hanigan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.01 / 2.30
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	105.583, 125.288, 103.988, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 20.1

The structure of Crystal Structure of Human GGT1 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Sodium atom in the Crystal Structure of Human GGT1 (pdb code 4z9o). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Human GGT1, PDB code: 4z9o:

Sodium binding site 1 out of 1 in the Crystal Structure of Human GGT1


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Human GGT1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Na1104 b:58.3 occ:1.00 O A:HOH882 2.8 56.3 1.0 O B:HOH1251 2.8 33.4 1.0 O B:ALA556 2.8 33.1 1.0 CD2 A:HIS36 3.4 43.3 1.0 CD B:LYS496 3.5 33.1 1.0 CB A:HIS36 3.6 45.9 1.0 CA B:ALA557 3.6 32.0 1.0 O B:HOH1286 3.7 52.4 1.0 CG A:HIS36 3.7 43.3 1.0 C B:ALA556 3.9 34.9 1.0 CB B:ALA557 3.9 29.4 1.0 CG B:LYS496 3.9 33.0 1.0 CB B:LYS496 4.0 34.5 1.0 CE B:LYS496 4.1 32.8 1.0 N B:ALA557 4.2 32.1 1.0 CG B:PRO566 4.3 34.0 1.0 NE2 A:HIS36 4.5 44.8 1.0 O A:ASN35 4.6 71.5 1.0 NZ B:LYS496 4.6 33.2 1.0 O B:HOH1325 4.6 54.0 1.0 CD B:PRO566 4.7 31.8 1.0 N B:SER558 4.7 29.2 1.0 C B:ALA557 4.8 31.0 1.0 CA B:LYS496 4.8 34.8 1.0 ND1 A:HIS36 4.8 44.6 1.0 CA A:HIS36 5.0 52.9 1.0

S.S.Terzyan, A.W.Burgett, A.Heroux, C.A.Smith, B.H.Mooers, M.H.Hanigan. Human Gamma-Glutamyl Transpeptidase 1: Structures of the Free Enzyme, Inhibitor-Bound Tetrahedral Transition States, and Glutamate-Bound Enzyme Reveal Novel Movement Within the Active Site During Catalysis. J.Biol.Chem. V. 290 17576 2015.
ISSN: ESSN 1083-351X
PubMed: 26013825
DOI: 10.1074/JBC.M115.659680