Zinc in PDB 3bvo: Crystal Structure of Human Co-Chaperone Protein Hscb

The structure of Crystal Structure of Human Co-Chaperone Protein Hscb, PDB code: 3bvo was solved by E.Bitto, C.A.Bingman, J.G.Mccoy, G.E.Wesenberg, G.N.Phillips Jr., Centerfor Eukaryotic Structural Genomics (Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.75 / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.644, 32.581, 114.362, 90.00, 105.24, 90.00
R / Rfree (%)	23.6 / 28.8

The binding sites of Zinc atom in the Crystal Structure of Human Co-Chaperone Protein Hscb (pdb code 3bvo). 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 Human Co-Chaperone Protein Hscb, PDB code: 3bvo:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Co-Chaperone Protein Hscb


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 Human Co-Chaperone Protein Hscb within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:63.9 occ:1.00 SG A:CYS58 2.3 71.9 1.0 SG A:CYS41 2.3 74.3 1.0 SG A:CYS61 2.3 67.2 1.0 SG A:CYS44 2.3 81.7 1.0 CB A:CYS58 3.2 69.8 1.0 CB A:CYS41 3.2 72.8 1.0 CB A:CYS44 3.3 74.6 1.0 CB A:CYS61 3.5 70.5 1.0 N A:CYS44 3.5 74.0 1.0 CA A:CYS44 4.0 74.5 1.0 N A:CYS61 4.1 71.2 1.0 CB A:ASN43 4.2 72.3 1.0 CA A:CYS61 4.3 71.2 1.0 C A:ASN43 4.5 73.1 1.0 CB A:GLN60 4.6 70.1 1.0 NE2 A:GLN65 4.6 70.2 1.0 CA A:CYS58 4.6 69.5 1.0 CA A:ASN43 4.7 72.1 1.0 CA A:CYS41 4.7 73.0 1.0 N A:ASN43 4.7 71.8 1.0 C A:GLN60 4.8 70.8 1.0 CB A:ALA63 4.9 71.0 1.0 N A:GLY46 5.0 74.9 1.0 C A:CYS61 5.0 71.3 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Co-Chaperone Protein Hscb


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 Human Co-Chaperone Protein Hscb within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:74.8 occ:1.00 SG B:CYS61 2.3 67.6 1.0 SG B:CYS44 2.3 81.9 1.0 SG B:CYS58 2.3 70.3 1.0 SG B:CYS41 2.3 75.2 1.0 N B:CYS44 3.3 74.9 1.0 CB B:CYS58 3.3 69.6 1.0 CB B:CYS61 3.4 70.5 1.0 CB B:CYS44 3.4 75.5 1.0 CB B:CYS41 3.5 73.8 1.0 CB B:ASN43 3.7 71.9 1.0 CA B:CYS44 3.9 75.2 1.0 N B:CYS61 4.0 71.6 1.0 C B:ASN43 4.1 73.7 1.0 CA B:CYS61 4.2 71.0 1.0 CA B:ASN43 4.3 72.3 1.0 N B:ASN43 4.4 71.3 1.0 CB B:GLN60 4.7 71.0 1.0 CA B:CYS58 4.7 69.3 1.0 CG B:ASN43 4.7 71.3 1.0 CB B:ALA63 4.8 72.8 1.0 C B:CYS61 4.8 70.9 1.0 ND2 B:ASN43 4.8 66.3 1.0 C B:GLN60 4.8 71.5 1.0 CA B:CYS41 4.9 73.4 1.0 N B:GLY45 4.9 75.3 1.0 C B:CYS44 5.0 75.4 1.0

E.Bitto, C.A.Bingman, L.Bittova, D.A.Kondrashov, R.M.Bannen, B.G.Fox, J.L.Markley, G.N.Phillips. Structure of Human J-Type Co-Chaperone Hscb Reveals A Tetracysteine Metal-Binding Domain. J.Biol.Chem. V. 283 30184 2008.
ISSN: ISSN 0021-9258
PubMed: 18713742
DOI: 10.1074/JBC.M804746200