Zinc in PDB 5tt5: Escherichia Coli Liga (K115M) in Complex with Nad+

All present enzymatic activity of Escherichia Coli Liga (K115M) in Complex with Nad+:
6.5.1.2;

The structure of Escherichia Coli Liga (K115M) in Complex with Nad+, PDB code: 5tt5 was solved by Y.Goldgur, M.-C.Unciuleac, S.H.Shuman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.48 / 1.55
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.907, 94.312, 150.927, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 20.5

The structure of Escherichia Coli Liga (K115M) in Complex with Nad+ also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Escherichia Coli Liga (K115M) in Complex with Nad+ (pdb code 5tt5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Escherichia Coli Liga (K115M) in Complex with Nad+, PDB code: 5tt5:

Zinc binding site 1 out of 1 in the Escherichia Coli Liga (K115M) in Complex with Nad+


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Escherichia Coli Liga (K115M) in Complex with Nad+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:19.5 occ:1.00 SG A:CYS408 2.3 18.1 1.0 SG A:CYS411 2.3 19.1 1.0 SG A:CYS426 2.3 18.4 1.0 SG A:CYS432 2.3 19.9 1.0 CB A:CYS408 3.1 17.2 1.0 CB A:CYS432 3.1 19.2 1.0 CB A:CYS426 3.3 19.1 1.0 CB A:CYS411 3.4 22.7 1.0 N A:CYS411 3.8 20.1 1.0 NE2 A:GLN435 4.0 20.9 1.0 CA A:CYS432 4.1 18.9 1.0 CA A:CYS411 4.2 20.3 1.0 CB A:VAL410 4.5 21.4 1.0 CA A:CYS408 4.5 22.7 1.0 CG1 A:VAL331 4.6 18.2 1.0 CA A:CYS426 4.7 17.6 1.0 C A:VAL410 4.8 21.7 1.0 CB A:SER413 4.9 17.8 1.0 C A:CYS411 4.9 20.2 1.0 OG A:SER413 4.9 21.3 1.0 N A:GLY412 4.9 20.1 1.0 O A:GLY428 4.9 21.8 1.0 N A:SER413 5.0 23.3 1.0 N A:VAL410 5.0 21.0 1.0

M.C.Unciuleac, Y.Goldgur, S.Shuman. Two-Metal Versus One-Metal Mechanisms of Lysine Adenylylation By Atp-Dependent and Nad(+)-Dependent Polynucleotide Ligases. Proc. Natl. Acad. Sci. V. 114 2592 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28223499
DOI: 10.1073/PNAS.1619220114