Zinc in PDB 2fpr: Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.

All present enzymatic activity of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.:
3.1.3.15;

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr was solved by E.S.Rangarajan, M.Cygler, A.Matte, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	53.256, 131.962, 106.140, 90.00, 90.00, 90.00
R / Rfree (%)	18.9 / 22

The structure of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Bromine	(Br)	7 atoms
Sodium	(Na)	1 atom

The binding sites of Zinc atom in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. (pdb code 2fpr). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model., PDB code: 2fpr:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:19.8 occ:1.00 ND1 A:HIS96 2.1 20.8 1.0 SG A:CYS104 2.2 23.2 1.0 SG A:CYS94 2.3 17.1 1.0 SG A:CYS102 2.3 23.6 1.0 CE1 A:HIS96 3.1 22.2 1.0 CG A:HIS96 3.1 19.9 1.0 CB A:CYS102 3.3 25.1 1.0 CB A:HIS96 3.5 19.2 1.0 CB A:CYS104 3.5 22.4 1.0 CB A:CYS94 3.5 17.1 1.0 N A:ARG105 3.6 20.4 1.0 C A:CYS104 3.8 21.6 1.0 N A:CYS104 3.8 23.4 1.0 CA A:CYS104 3.8 22.4 1.0 CA A:CYS94 4.1 17.1 1.0 N A:HIS96 4.1 18.3 1.0 NE2 A:HIS96 4.2 22.0 1.0 CA A:ARG105 4.2 19.4 1.0 CD2 A:HIS96 4.3 21.9 1.0 CD A:PRO95 4.3 17.7 1.0 CB A:ARG105 4.3 19.5 1.0 CA A:HIS96 4.4 19.0 1.0 O A:CYS104 4.5 21.2 1.0 C A:CYS94 4.5 17.1 1.0 N A:PRO95 4.5 17.4 1.0 O A:HOH544 4.5 20.2 1.0 CA A:CYS102 4.7 25.0 1.0 C A:CYS102 4.9 24.9 1.0 N A:ASP103 4.9 24.9 1.0 O A:HOH566 5.0 24.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure the N-Terminal Domain of E. Coli Hisb. Apo Mg Model. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn501 b:11.9 occ:1.00 ND1 B:HIS96 2.1 12.1 1.0 SG B:CYS94 2.3 11.2 1.0 SG B:CYS102 2.3 13.4 1.0 SG B:CYS104 2.3 12.7 1.0 CE1 B:HIS96 3.0 11.2 1.0 CG B:HIS96 3.1 11.3 1.0 CB B:CYS102 3.2 12.6 1.0 CB B:CYS94 3.4 11.4 1.0 CB B:HIS96 3.5 11.5 1.0 N B:ARG105 3.5 11.1 1.0 CB B:CYS104 3.5 11.7 1.0 C B:CYS104 3.7 11.2 1.0 CA B:CYS104 3.8 11.4 1.0 N B:CYS104 3.8 11.6 1.0 CA B:CYS94 4.0 11.1 1.0 CA B:ARG105 4.2 11.0 1.0 NE2 B:HIS96 4.2 10.9 1.0 N B:HIS96 4.2 11.5 1.0 CD2 B:HIS96 4.2 11.1 1.0 CB B:ARG105 4.3 11.0 1.0 CD B:PRO95 4.4 10.8 1.0 CA B:HIS96 4.5 11.8 1.0 O B:CYS104 4.5 10.2 1.0 C B:CYS94 4.5 10.9 1.0 O B:HOH562 4.5 16.6 1.0 N B:PRO95 4.6 10.6 1.0 CA B:CYS102 4.6 12.6 1.0 C B:CYS102 4.8 12.5 1.0 N B:ASP103 4.9 12.0 1.0

E.S.Rangarajan, A.Proteau, J.Wagner, M.N.Hung, A.Matte, M.Cygler. Structural Snapshots of Escherichia Coli Histidinol Phosphate Phosphatase Along the Reaction Pathway. J.Biol.Chem. V. 281 37930 2006.
ISSN: ISSN 0021-9258
PubMed: 16966333
DOI: 10.1074/JBC.M604916200