Zinc in PDB 2gmw: Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli.

The structure of Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli., PDB code: 2gmw was solved by K.Zhang, G.Deleon, G.D.Wright, M.S.Junop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.50
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.904, 63.977, 103.324, 90.00, 90.00, 90.00
R / Rfree (%)	16.3 / 21.2

The binding sites of Zinc atom in the Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli. (pdb code 2gmw). 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 of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli., PDB code: 2gmw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:21.8 occ:1.00 ND1 A:HIS114 2.1 21.2 1.0 SG A:CYS112 2.3 19.5 1.0 SG A:CYS127 2.3 20.5 1.0 SG A:CYS129 2.3 20.4 1.0 CE1 A:HIS114 3.0 21.4 1.0 CG A:HIS114 3.1 19.6 1.0 CB A:CYS127 3.3 20.3 1.0 CB A:CYS112 3.4 18.7 1.0 CB A:CYS129 3.5 20.4 1.0 CB A:HIS114 3.5 18.3 1.0 N A:ARG130 3.6 19.4 1.0 C A:CYS129 3.8 19.6 1.0 CA A:CYS129 3.8 20.8 1.0 N A:CYS129 3.9 20.6 1.0 CA A:CYS112 4.0 19.2 1.0 NE2 A:HIS114 4.2 22.0 1.0 CD2 A:HIS114 4.2 20.5 1.0 CA A:ARG130 4.3 19.7 1.0 N A:HIS114 4.3 17.7 1.0 CB A:ARG130 4.4 19.8 1.0 CD A:PRO113 4.5 19.1 1.0 O A:CYS129 4.5 19.0 1.0 O A:HOH369 4.5 21.5 1.0 CA A:HIS114 4.5 17.9 1.0 C A:CYS112 4.6 18.4 1.0 CA A:CYS127 4.6 20.4 1.0 N A:PRO113 4.7 18.5 1.0 O A:HOH318 4.8 13.6 1.0 O A:HOH370 4.8 21.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of D,D-Heptose 1.7-Bisphosphate Phosphatase From E. Coli. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn300 b:19.1 occ:1.00 ND1 B:HIS114 2.1 17.4 1.0 SG B:CYS112 2.3 17.4 1.0 SG B:CYS129 2.3 19.2 1.0 SG B:CYS127 2.3 18.5 1.0 CE1 B:HIS114 3.0 17.1 1.0 CG B:HIS114 3.1 15.4 1.0 CB B:CYS127 3.3 19.9 1.0 CB B:CYS112 3.3 17.1 1.0 CB B:CYS129 3.4 20.8 1.0 CB B:HIS114 3.4 18.8 1.0 N B:ARG130 3.6 18.3 1.0 C B:CYS129 3.8 18.9 1.0 CA B:CYS129 3.8 20.6 1.0 N B:CYS129 3.9 20.5 1.0 CA B:CYS112 4.0 17.5 1.0 NE2 B:HIS114 4.2 16.8 1.0 CD2 B:HIS114 4.2 20.8 1.0 CB B:ARG130 4.2 17.7 1.0 CA B:ARG130 4.3 19.0 1.0 N B:HIS114 4.3 18.4 1.0 CD B:PRO113 4.4 17.2 1.0 C B:CYS112 4.5 16.2 1.0 CA B:HIS114 4.5 18.2 1.0 O B:HOH325 4.5 28.9 1.0 O B:CYS129 4.5 19.2 1.0 N B:PRO113 4.6 17.0 1.0 CA B:CYS127 4.7 20.5 1.0 O B:HOH317 4.8 14.6 1.0 C B:CYS127 5.0 21.7 1.0

P.L.Taylor, S.Sugiman-Marangos, K.Zhang, M.A.Valvano, G.D.Wright, M.S.Junop. Structural and Kinetic Characterization of the Lps Biosynthetic Enzyme D-Alpha,Beta-D-Heptose-1,7-Bisphosphate Phosphatase (Gmhb) From Escherichia Coli. Biochemistry V. 49 1033 2010.
ISSN: ISSN 0006-2960
PubMed: 20050699
DOI: 10.1021/BI901780J