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Sodium in PDB 4zcg: Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate)

Enzymatic activity of Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate)

All present enzymatic activity of Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate):
2.3.2.2; 3.4.19.13; 3.4.19.14;

Protein crystallography data

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

Resolution Low / High (Å) 40.02 / 2.22
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 105.242, 125.230, 104.061, 90.00, 90.00, 90.00
R / Rfree (%) 14.6 / 18.5

Other elements in 4zcg:

The structure of Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate) also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate) (pdb code 4zcg). 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 in Complex with Glutamate (with All Atoms of Glutamate), PDB code: 4zcg:

Sodium binding site 1 out of 1 in 4zcg

Go back to Sodium Binding Sites List in 4zcg
Sodium binding site 1 out of 1 in the Crystal Structure of Human GGT1 in Complex with Glutamate (with All Atoms of Glutamate)


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 in Complex with Glutamate (with All Atoms of Glutamate) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na608

b:52.8
occ:1.00
O A:HOH934 2.7 47.4 1.0
O B:ALA556 2.7 28.6 1.0
O B:HOH1235 3.0 27.5 1.0
CD2 A:HIS36 3.3 40.8 1.0
O B:HOH1278 3.4 45.2 1.0
CB A:HIS36 3.5 44.6 1.0
CG A:HIS36 3.6 42.2 1.0
CA B:ALA557 3.7 26.5 1.0
CD B:LYS496 3.7 33.5 1.0
C B:ALA556 3.8 28.7 1.0
CB B:ALA557 3.9 28.1 1.0
CG B:LYS496 4.1 32.2 1.0
CB B:LYS496 4.1 31.5 1.0
CE B:LYS496 4.2 33.5 1.0
N B:ALA557 4.2 26.3 1.0
O A:ASN35 4.3 62.7 1.0
NE2 A:HIS36 4.4 41.7 1.0
CG B:PRO566 4.5 28.7 1.0
NZ B:LYS496 4.6 32.1 1.0
O B:HOH1306 4.7 46.1 1.0
ND1 A:HIS36 4.8 43.5 1.0
CD B:PRO566 4.9 28.7 1.0
CA B:LYS496 4.9 30.2 1.0
C B:ALA557 4.9 25.8 1.0
N B:SER558 4.9 25.3 1.0
CA A:HIS36 4.9 49.5 1.0

Reference:

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
Page generated: Tue Dec 15 10:06:39 2020

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