Zinc in PDB 4dxc: Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group

All present enzymatic activity of Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group:
3.5.2.6;

The structure of Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group, PDB code: 4dxc was solved by F.Van Den Akker, W.Ke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.32 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.450, 47.844, 108.288, 90.00, 114.14, 90.00
R / Rfree (%)	23.3 / 29.1

The binding sites of Zinc atom in the Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group (pdb code 4dxc). 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 the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group, PDB code: 4dxc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group


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 the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:38.5 occ:1.00 NE2 A:HIS468 2.2 22.4 1.0 OE2 A:GLU477 2.4 31.6 1.0 OD1 A:ASP164 2.5 36.2 1.0 OD2 A:ASP164 2.5 35.6 1.0 O A:HOH877 2.6 61.2 1.0 CG A:ASP164 2.8 35.7 1.0 CD2 A:HIS468 3.1 22.1 1.0 CE1 A:HIS468 3.2 21.3 1.0 O A:HOH856 3.3 39.6 1.0 O A:HOH875 3.3 38.9 1.0 CD A:GLU477 3.4 29.2 1.0 OE1 A:GLU477 3.9 30.2 1.0 O A:ASP164 3.9 36.3 1.0 CG A:HIS468 4.2 22.7 1.0 ND1 A:HIS468 4.3 21.7 1.0 CB A:ASP164 4.3 35.3 1.0 CG A:GLU477 4.6 25.3 1.0 NE2 A:GLN253 4.7 34.6 1.0 CD A:LYS251 4.7 29.9 1.0 C A:ASP164 4.8 36.0 1.0 CA A:ASP164 5.0 35.2 1.0 CG A:MET473 5.0 20.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group


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 the Engineered Mbp Tem-1 Fusion Protein RG13, C2 Space Group within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn702 b:43.2 occ:1.00 ND1 A:HIS514 2.0 27.6 1.0 ND1 A:HIS509 2.0 29.9 1.0 O A:HOH890 2.5 36.2 1.0 O A:HOH857 2.7 39.6 1.0 CE1 A:HIS514 2.9 29.2 1.0 CE1 A:HIS509 2.9 30.7 1.0 CG A:HIS509 3.0 29.4 1.0 CG A:HIS514 3.1 27.7 1.0 CB A:HIS509 3.4 27.5 1.0 CB A:HIS514 3.5 26.3 1.0 CA A:HIS514 4.0 26.0 1.0 NE2 A:HIS514 4.0 29.1 1.0 NE2 A:HIS509 4.1 31.2 1.0 CD2 A:HIS509 4.1 31.0 1.0 CD2 A:HIS514 4.1 28.6 1.0 CA A:HIS509 4.2 27.3 1.0 O A:HIS509 4.6 27.8 1.0 C A:HIS509 4.8 27.6 1.0 N A:HIS514 4.9 26.2 1.0

W.Ke, A.H.Laurent, M.D.Armstrong, Y.Chen, W.E.Smith, J.Liang, C.M.Wright, M.Ostermeier, F.Van Den Akker. Structure of An Engineered Beta-Lactamase Maltose Binding Protein Fusion Protein: Insights Into Heterotropic Allosteric Regulation. Plos One V. 7 39168 2012.
ISSN: ESSN 1932-6203
PubMed: 22720063
DOI: 10.1371/JOURNAL.PONE.0039168