Zinc in PDB 3kvt: Tetramerization Domain From AKV3.1 (Shaw-Subfamily) Voltage-Gated Potassium Channel

The structure of Tetramerization Domain From AKV3.1 (Shaw-Subfamily) Voltage-Gated Potassium Channel, PDB code: 3kvt was solved by K.A.Bixby, M.H.Nanao, N.V.Shen, A.Kreusch, H.Bellamy, P.J.Pfaffinger, S.Choe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.00
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.191, 67.191, 138.900, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 23.8

The binding sites of Zinc atom in the Tetramerization Domain From AKV3.1 (Shaw-Subfamily) Voltage-Gated Potassium Channel (pdb code 3kvt). 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 Tetramerization Domain From AKV3.1 (Shaw-Subfamily) Voltage-Gated Potassium Channel, PDB code: 3kvt:

Zinc binding site 1 out of 1 in the Tetramerization Domain From AKV3.1 (Shaw-Subfamily) 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 Tetramerization Domain From AKV3.1 (Shaw-Subfamily) Voltage-Gated Potassium Channel within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn179 b:31.0 occ:1.00 SG A:CYS103 2.3 28.5 1.0 ND1 A:HIS75 2.3 23.3 1.0 SG A:CYS102 2.5 33.9 1.0 CE1 A:HIS75 3.2 23.3 1.0 CG A:HIS75 3.3 23.1 1.0 CB A:HIS75 3.6 20.8 1.0 CB A:CYS103 3.6 33.2 1.0 CB A:CYS102 3.6 32.9 1.0 N A:CYS103 3.8 34.2 1.0 C A:CYS102 3.9 32.4 1.0 CA A:HIS75 4.1 22.1 1.0 CA A:CYS103 4.2 35.6 1.0 NE2 A:HIS75 4.3 23.7 1.0 CB A:GLU100 4.3 40.4 1.0 O A:CYS102 4.3 33.8 1.0 CA A:CYS102 4.3 33.2 1.0 CD2 A:HIS75 4.4 21.9 1.0 N A:TYR76 4.9 24.4 1.0 N A:CYS102 4.9 33.4 1.0

K.A.Bixby, M.H.Nanao, N.V.Shen, A.Kreusch, H.Bellamy, P.J.Pfaffinger, S.Choe. ZN2+-Binding and Molecular Determinants of Tetramerization in Voltage-Gated K+ Channels. Nat.Struct.Biol. V. 6 38 1999.
ISSN: ISSN 1072-8368
PubMed: 9886290
DOI: 10.1038/4911