Zinc in PDB 3gky: The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape

The structure of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape, PDB code: 3gky was solved by M.Liu, Z.L.Wan, Y.C.Chu, H.Alddin, B.Klaproth, M.A.Weiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	22.58 / 1.80
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	78.225, 78.225, 36.712, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 25.3

The structure of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape (pdb code 3gky). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape, PDB code: 3gky:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn31 b:28.9 occ:0.33 NE2 B:HIS10 2.1 20.4 1.0 CL B:CL32 2.3 38.9 0.3 CE1 B:HIS10 3.0 21.9 1.0 CD2 B:HIS10 3.1 22.8 1.0 O B:HOH89 4.0 51.1 1.0 ND1 B:HIS10 4.2 25.7 1.0 CG B:HIS10 4.2 22.1 1.0 O B:HOH34 4.6 34.9 1.0

Zinc binding site 2 out of 2 in the The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Structural Basis of An Er Stress-Associated Bottleneck in A Protein Folding Landscape within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn31 b:19.7 occ:0.33 NE2 D:HIS10 2.1 21.7 1.0 CL D:CL32 2.2 20.7 0.3 CE1 D:HIS10 2.9 26.1 1.0 CD2 D:HIS10 3.1 20.9 1.0 ND1 D:HIS10 4.1 27.6 1.0 CG D:HIS10 4.2 23.1 1.0 CB D:LEU6 4.8 23.3 1.0 O D:LEU6 4.8 23.6 1.0

M.Liu, Z.L.Wan, Y.C.Chu, H.Aladdin, B.Klaproth, M.Choquette, Q.X.Hua, R.B.Mackin, J.S.Rao, P.De Meyts, P.G.Katsoyannis, P.Arvan, M.A.Weiss. Crystal Structure of A "Nonfoldable" Insulin: Impaired Folding Efficiency Despite Native Activity. J.Biol.Chem. V. 284 35259 2009.
ISSN: ISSN 0021-9258
PubMed: 19850922
DOI: 10.1074/JBC.M109.046888