Zinc in PDB 2vqx: Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans.

The structure of Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans., PDB code: 2vqx was solved by W.R.Melik-Adamyan, I.P.Kuranova, K.M.Polyakov, I.V.Demidyuk, T.Y.Gromova, S.V.Kostrov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.63 / 1.82
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	70.760, 78.650, 59.280, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 20.2

The binding sites of Zinc atom in the Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans. (pdb code 2vqx). 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 Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans., PDB code: 2vqx:

Zinc binding site 1 out of 1 in the Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Precursor of Protealysin, Metalloproteinase From Serratia Proteamaculans. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1342 b:15.8 occ:0.50 O A:HOH2276 2.1 12.0 0.5 NE2 A:HIS166 2.1 13.1 1.0 OE2 A:GLU186 2.1 16.7 1.0 O A:HOH2277 2.2 21.0 0.5 NE2 A:HIS162 2.2 13.7 1.0 CE1 A:HIS166 2.9 12.3 1.0 CD A:GLU186 3.0 15.4 1.0 CE1 A:HIS162 3.2 12.3 1.0 CD2 A:HIS162 3.2 12.6 1.0 OE1 A:GLU186 3.2 17.5 1.0 CD2 A:HIS166 3.2 12.9 1.0 O A:HOH2002 3.6 24.1 1.0 O A:HOH2007 4.0 22.7 1.0 ND1 A:HIS166 4.1 12.0 1.0 ND1 A:HIS162 4.3 12.1 1.0 CG A:HIS162 4.3 11.0 1.0 CG A:HIS166 4.3 11.1 1.0 CG A:GLU186 4.3 11.7 1.0 CB A:SER189 4.4 8.0 1.0 OH A:TYR177 4.5 17.5 1.0 OG A:SER189 4.5 9.5 1.0 CA A:GLU186 4.8 9.0 1.0 CB A:ARG7 4.9 25.9 1.0 O A:SER8 5.0 23.8 1.0

I.V.Demidyuk, T.Y.Gromova, K.M.Polyakov, W.R.Melik-Adamyan, I.P.Kuranova, S.V.Kostrov. Crystal Structure of the Protealysin Precursor: Insights Into Propeptide Function. J.Biol.Chem. V. 285 2003 2010.
ISSN: ISSN 0021-9258
PubMed: 19915005
DOI: 10.1074/JBC.M109.015396