Zinc in PDB 1nn7: Crystal Structure of the Tetramerization Domain of the Shal Voltage- Gated Potassium Channel

The structure of Crystal Structure of the Tetramerization Domain of the Shal Voltage- Gated Potassium Channel, PDB code: 1nn7 was solved by W.Zhou, S.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.40 / 2.10
Space group	P 4 21 2
Cell size a, b, c (Å), α, β, γ (°)	59.999, 59.999, 61.593, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 27.7

The binding sites of Zinc atom in the Crystal Structure of the Tetramerization Domain of the Shal Voltage- Gated Potassium Channel (pdb code 1nn7). 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 Crystal Structure of the Tetramerization Domain of the Shal Voltage- Gated Potassium Channel, PDB code: 1nn7:

Zinc binding site 1 out of 1 in the Crystal Structure of the Tetramerization Domain of the Shal Voltage- Gated Potassium Channel


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 Tetramerization Domain of the Shal Voltage- Gated Potassium Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:26.1 occ:1.00 ND1 A:HIS105 2.1 19.7 1.0 SG A:CYS132 2.2 25.6 1.0 SG A:CYS133 2.2 25.6 1.0 CE1 A:HIS105 2.9 19.4 1.0 CB A:CYS132 3.3 27.6 1.0 CG A:HIS105 3.3 18.6 1.0 CB A:CYS133 3.4 25.0 1.0 N A:CYS133 3.6 28.0 1.0 CB A:HIS105 3.8 22.5 1.0 C A:CYS132 3.8 27.4 1.0 CA A:CYS133 4.0 27.6 1.0 CA A:HIS105 4.0 23.4 1.0 NE2 A:HIS105 4.1 21.0 1.0 CA A:CYS132 4.1 28.4 1.0 CD2 A:HIS105 4.3 20.2 1.0 O A:CYS132 4.3 27.8 1.0 N A:CYS132 4.8 28.6 1.0 O A:LEU104 4.8 26.4 1.0 N A:TYR106 4.8 23.5 1.0

M.H.Nanao, W.Zhou, P.J.Pfaffinger, S.Choe. Determining the Basis of Channel-Tetramerization Specificity By X-Ray Crystallography and A Sequence-Comparison Algorithm: Family Values (Famval) Proc.Natl.Acad.Sci.Usa V. 100 8670 2003.
ISSN: ISSN 0027-8424
PubMed: 12835418
DOI: 10.1073/PNAS.1432840100