Zinc in PDB 2bh7: Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms

All present enzymatic activity of Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms:
3.5.1.28;

The structure of Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms, PDB code: 2bh7 was solved by S.Petrella, R.Herman, E.Sauvage, C.Genereux, A.Pennartz, B.Joris, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.77 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	88.990, 88.990, 183.923, 90.00, 90.00, 120.00
R / Rfree (%)	23.1 / 27.9

The binding sites of Zinc atom in the Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms (pdb code 2bh7). 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 Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms, PDB code: 2bh7:

Zinc binding site 1 out of 1 in the Crystal Structure of A Semet Derivative of Amid at 2.2 Angstroms


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 A Semet Derivative of Amid at 2.2 Angstroms within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:24.0 occ:1.00 O A:HOH2145 2.1 11.5 1.0 OD1 A:ASP161 2.2 24.3 1.0 ND1 A:HIS151 2.2 16.4 1.0 ND1 A:HIS35 2.5 20.8 1.0 CG A:ASP161 3.1 23.1 1.0 CG A:HIS151 3.1 14.1 1.0 CB A:HIS35 3.2 20.7 1.0 CG A:HIS35 3.2 22.8 1.0 CE1 A:HIS151 3.2 14.6 1.0 OD2 A:ASP161 3.3 24.2 1.0 CB A:HIS151 3.4 15.3 1.0 CE1 A:HIS35 3.6 21.4 1.0 O A:HOH2050 3.6 44.1 1.0 CA A:HIS35 4.0 21.6 1.0 O A:HOH2034 4.2 42.4 1.0 CD2 A:HIS151 4.3 14.7 1.0 NE2 A:HIS151 4.3 15.2 1.0 CE A:LYS159 4.3 23.9 1.0 O A:HIS84 4.4 26.5 1.0 CB A:ASP161 4.4 22.2 1.0 OE2 A:GLU104 4.4 32.0 1.0 CD2 A:HIS35 4.4 22.8 1.0 NE2 A:HIS35 4.6 22.8 1.0 N A:TYR36 4.8 22.0 1.0 O A:TYR36 4.8 22.6 1.0 NZ A:LYS159 4.9 24.3 1.0 CA A:HIS151 4.9 17.7 1.0 C A:HIS35 5.0 22.2 1.0

F.Kerff, S.Petrella, F.Mercier, E.Sauvage, R.Herman, A.Pennartz, A.Zervosen, A.Luxen, J.M.Frere, B.Joris, P.Charlier. Specific Structural Features of the N-Acetylmuramoyl-L-Alanine Amidase Amid From Escherichia Coli and Mechanistic Implications For Enzymes of This Family. J.Mol.Biol. V. 397 249 2010.
ISSN: ISSN 0022-2836
PubMed: 20036252
DOI: 10.1016/J.JMB.2009.12.038