Zinc in PDB 2bb0: Structure of Imidazolonepropionase From Bacillus Subtilis

All present enzymatic activity of Structure of Imidazolonepropionase From Bacillus Subtilis:
3.5.2.7;

The structure of Structure of Imidazolonepropionase From Bacillus Subtilis, PDB code: 2bb0 was solved by Y.H.Liang, Y.Yu, X.D.Su, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.730, 106.340, 66.470, 90.00, 89.92, 90.00
R / Rfree (%)	18.8 / 22.1

The binding sites of Zinc atom in the Structure of Imidazolonepropionase From Bacillus Subtilis (pdb code 2bb0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Imidazolonepropionase From Bacillus Subtilis, PDB code: 2bb0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Imidazolonepropionase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Imidazolonepropionase From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1601 b:14.8 occ:1.00 NE2 A:HIS82 2.2 10.0 1.0 NE2 A:HIS80 2.2 11.1 1.0 NE2 A:HIS249 2.3 5.4 1.0 OD1 A:ASP324 2.3 8.4 1.0 O A:HOH1729 2.4 23.9 1.0 CD2 A:HIS249 3.1 5.3 1.0 CE1 A:HIS82 3.1 11.5 1.0 CE1 A:HIS80 3.1 9.9 1.0 CD2 A:HIS82 3.2 9.8 1.0 CD2 A:HIS80 3.2 8.6 1.0 CG A:ASP324 3.3 10.2 1.0 CE1 A:HIS249 3.3 7.1 1.0 OD2 A:ASP324 3.6 10.3 1.0 ND1 A:HIS82 4.3 11.9 1.0 ND1 A:HIS80 4.3 8.9 1.0 CG A:HIS249 4.3 7.4 1.0 CG A:HIS82 4.3 10.9 1.0 CG A:HIS80 4.3 8.8 1.0 ND1 A:HIS249 4.3 6.7 1.0 O A:HOH1730 4.4 17.8 1.0 CD1 A:LEU294 4.5 9.1 1.0 CB A:ASP324 4.6 8.9 1.0 CE A:LYS149 4.6 12.6 1.0 CD A:LYS149 4.8 12.7 1.0 ND2 A:ASN326 4.9 9.0 1.0 CA A:ASP324 4.9 8.5 1.0

Zinc binding site 2 out of 2 in the Structure of Imidazolonepropionase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Imidazolonepropionase From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2601 b:14.6 occ:1.00 NE2 B:HIS82 2.2 14.1 1.0 NE2 B:HIS80 2.2 9.6 1.0 O B:HOH2714 2.3 16.8 1.0 OD1 B:ASP324 2.3 11.1 1.0 NE2 B:HIS249 2.4 10.7 1.0 CD2 B:HIS249 3.1 10.1 1.0 CE1 B:HIS82 3.1 12.4 1.0 CD2 B:HIS80 3.2 8.1 1.0 CD2 B:HIS82 3.2 11.8 1.0 CE1 B:HIS80 3.2 5.8 1.0 CG B:ASP324 3.3 12.2 1.0 CE1 B:HIS249 3.5 11.3 1.0 OD2 B:ASP324 3.7 10.5 1.0 ND1 B:HIS82 4.3 12.1 1.0 ND1 B:HIS80 4.3 5.2 1.0 CG B:HIS82 4.3 11.2 1.0 CG B:HIS80 4.3 7.5 1.0 CG B:HIS249 4.3 11.5 1.0 ND1 B:HIS249 4.5 10.2 1.0 CD1 B:LEU294 4.5 9.1 1.0 CB B:ASP324 4.6 10.9 1.0 O B:HOH2715 4.6 24.8 1.0 CE B:LYS149 4.6 9.5 1.0 CD B:LYS149 4.8 12.2 1.0 CA B:ASP324 4.9 9.8 1.0 ND2 B:ASN326 5.0 13.2 1.0

Y.Yu, Y.H.Liang, E.Brostromer, J.M.Quan, S.Panjikar, Y.H.Dong, X.D.Su. A Catalytic Mechanism Revealed By the Crystal Structures of the Imidazolonepropionase From Bacillus Subtilis J.Biol.Chem. V. 281 36929 2006.
ISSN: ISSN 0021-9258
PubMed: 16990261
DOI: 10.1074/JBC.M607703200