Zinc in PDB 1hxp: Nucleotide Transferase

All present enzymatic activity of Nucleotide Transferase:
2.7.7.10;

The structure of Nucleotide Transferase, PDB code: 1hxp was solved by J.E.Wedekind, P.A.Frey, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.600, 217.200, 69.600, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Nucleotide Transferase also contains other interesting chemical elements:

Iron

(Fe)

2 atoms

The binding sites of Zinc atom in the Nucleotide Transferase (pdb code 1hxp). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Nucleotide Transferase, PDB code: 1hxp:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Nucleotide Transferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Nucleotide Transferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn350 b:21.4 occ:1.00 ND1 A:HIS164 2.0 19.8 1.0 ND1 A:HIS115 2.0 20.2 1.0 SG A:CYS52 2.2 17.5 1.0 SG A:CYS55 2.4 21.6 1.0 CB A:CYS52 2.9 18.4 1.0 CE1 A:HIS115 2.9 18.0 1.0 CG A:HIS164 3.0 20.9 1.0 CE1 A:HIS164 3.0 15.9 1.0 CG A:HIS115 3.1 23.9 1.0 CB A:HIS164 3.4 20.1 1.0 CB A:CYS55 3.4 18.0 1.0 N A:CYS55 3.5 14.9 1.0 CB A:HIS115 3.6 25.7 1.0 CA A:CYS55 3.8 18.1 1.0 CD2 A:HIS164 4.1 16.5 1.0 NE2 A:HIS164 4.1 17.8 1.0 NE2 A:HIS115 4.1 17.1 1.0 CA A:HIS115 4.1 19.7 1.0 C A:LEU54 4.2 16.1 1.0 CD2 A:HIS115 4.2 19.5 1.0 CA A:CYS52 4.4 28.5 1.0 CA A:HIS164 4.4 27.0 1.0 CB A:LEU54 4.5 14.3 1.0 CA A:LEU54 4.7 19.5 1.0 CB A:ASP49 4.7 25.6 1.0 N A:LEU54 4.7 20.0 1.0 C A:CYS52 4.8 26.6 1.0 OD1 A:ASN162 4.8 39.0 1.0 O A:LEU54 4.8 16.5 1.0 N A:ASP49 4.9 27.9 1.0 O A:CYS52 4.9 26.1 1.0 N A:HIS115 5.0 17.5 1.0

Zinc binding site 2 out of 2 in the Nucleotide Transferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Nucleotide Transferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn349 b:24.8 occ:1.00 ND1 B:HIS164 2.0 20.3 1.0 ND1 B:HIS115 2.1 27.1 1.0 SG B:CYS52 2.3 23.4 1.0 SG B:CYS55 2.3 24.4 1.0 CG B:HIS164 3.0 23.8 1.0 CE1 B:HIS115 3.0 22.4 1.0 CE1 B:HIS164 3.0 17.3 1.0 CB B:CYS52 3.0 23.2 1.0 CG B:HIS115 3.1 31.0 1.0 CB B:CYS55 3.4 23.4 1.0 CB B:HIS164 3.4 27.4 1.0 CB B:HIS115 3.5 22.4 1.0 N B:CYS55 3.6 16.2 1.0 CA B:CYS55 3.7 25.9 1.0 CA B:HIS115 4.1 21.9 1.0 CD2 B:HIS164 4.1 24.3 1.0 NE2 B:HIS115 4.1 26.7 1.0 NE2 B:HIS164 4.1 18.7 1.0 C B:LEU54 4.2 19.8 1.0 CD2 B:HIS115 4.2 31.1 1.0 CA B:HIS164 4.4 25.9 1.0 CA B:CYS52 4.5 26.6 1.0 CB B:ASP49 4.6 26.8 1.0 CB B:LEU54 4.6 16.9 1.0 N B:LEU54 4.7 18.3 1.0 CA B:LEU54 4.7 16.8 1.0 OD1 B:ASN162 4.7 42.6 1.0 O B:LEU54 4.7 22.5 1.0 N B:ASP49 4.8 34.3 1.0 C B:CYS52 4.8 25.4 1.0 O B:HOH395 4.9 30.2 1.0 O B:CYS52 5.0 24.1 1.0 N B:HIS115 5.0 19.1 1.0

J.E.Wedekind, P.A.Frey, I.Rayment. Three-Dimensional Structure of Galactose-1-Phosphate Uridylyltransferase From Escherichia Coli at 1.8 A Resolution. Biochemistry V. 34 11049 1995.
ISSN: ISSN 0006-2960
PubMed: 7669762
DOI: 10.1021/BI00035A010