Zinc in PDB 1vzy: Crystal Structure of the Bacillus Subtilis HSP33

The structure of Crystal Structure of the Bacillus Subtilis HSP33, PDB code: 1vzy was solved by I.K.Janda, Y.Devedjiev, U.Derewenda, Z.Dauter, J.Bielnicki, D.R.Cooper, A.Joachimiak, Z.S.Derewenda, Midwest Center For Structural Genomics(Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.97
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	115.292, 115.292, 106.441, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 22.5

The binding sites of Zinc atom in the Crystal Structure of the Bacillus Subtilis HSP33 (pdb code 1vzy). 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 Bacillus Subtilis HSP33, PDB code: 1vzy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the Bacillus Subtilis HSP33


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 Bacillus Subtilis HSP33 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1291 b:29.9 occ:1.00 SG A:CYS235 2.2 25.5 1.0 SG A:CYS237 2.3 24.9 1.0 SG A:CYS271 2.3 25.2 1.0 SG A:CYS268 2.4 27.5 1.0 CB A:CYS235 3.1 26.1 1.0 CB A:CYS268 3.2 28.8 1.0 CB A:CYS237 3.2 27.3 1.0 CB A:CYS271 3.4 24.4 1.0 N A:CYS271 3.9 24.8 1.0 O A:HOH2125 4.1 25.1 1.0 CA A:CYS271 4.2 26.3 1.0 N A:CYS237 4.2 26.7 1.0 CA A:CYS237 4.3 27.4 1.0 O A:HOH2124 4.3 23.4 1.0 CA A:CYS235 4.4 25.5 1.0 O A:CYS235 4.5 25.2 1.0 CB A:PHE270 4.5 28.4 1.0 O A:HOH2128 4.5 37.9 1.0 C A:CYS235 4.6 24.9 1.0 CA A:CYS268 4.7 27.3 1.0 C A:PHE270 4.8 26.7 1.0 CB A:GLU273 4.8 26.7 1.0 C A:CYS271 4.9 26.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the Bacillus Subtilis HSP33


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 Bacillus Subtilis HSP33 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1287 b:33.2 occ:1.00 SG B:CYS235 2.2 30.6 1.0 SG B:CYS271 2.2 28.0 1.0 SG B:CYS268 2.3 29.1 1.0 SG B:CYS237 2.4 35.4 1.0 CB B:CYS268 3.3 28.4 1.0 CB B:CYS235 3.3 33.6 1.0 CB B:CYS271 3.3 26.3 1.0 CB B:CYS237 3.4 37.1 1.0 N B:CYS271 3.8 24.1 1.0 CA B:CYS271 4.1 26.6 1.0 N B:CYS237 4.3 38.0 1.0 CA B:CYS237 4.4 37.1 1.0 O B:HOH2118 4.5 34.2 1.0 CA B:CYS235 4.6 33.2 1.0 O B:CYS235 4.6 36.9 1.0 CB B:PHE270 4.6 25.2 1.0 C B:CYS235 4.6 36.2 1.0 CA B:CYS268 4.7 29.2 1.0 C B:PHE270 4.7 25.2 1.0 C B:CYS271 4.8 28.4 1.0 N B:ASN272 5.0 29.3 1.0 CG B:GLU273 5.0 44.4 1.0 NH1 B:ARG86 5.0 30.2 1.0

I.Janda, Y.Devedjiev, U.Derewenda, Z.Dauter, J.Bielnicki, D.R.Cooper, P.C.Graf, A.Joachimiak, U.Jakob, Z.S.Derewenda. The Crystal Structure of the Reduced, ZN2+-Bound Form of the B. Subtilis HSP33 Chaperone and Its Implications For the Activation Mechanism. Structure V. 12 1901 2004.
ISSN: ISSN 0969-2126
PubMed: 15458638
DOI: 10.1016/J.STR.2004.08.003