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Nickel in PDB 3bj4: The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction

Protein crystallography data

The structure of The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction, PDB code: 3bj4 was solved by R.Wiener, J.A.Hirsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.46 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 51.321, 51.321, 71.094, 90.00, 90.00, 120.00
R / Rfree (%) 22.1 / 25.5

Nickel Binding Sites:

The binding sites of Nickel atom in the The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction (pdb code 3bj4). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction, PDB code: 3bj4:

Nickel binding site 1 out of 1 in 3bj4

Go back to Nickel Binding Sites List in 3bj4
Nickel binding site 1 out of 1 in the The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of The KCNQ1 (KV7.1) C-Terminus, A Multi-Tiered Scaffold For Subunit Assembly and Protein Interaction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni1

b:23.6
occ:0.25
NE2 A:HIS620 2.2 30.8 1.0
NE2 B:HIS620 2.2 27.0 1.0
O B:HOH632 2.4 17.2 0.5
CE1 A:HIS620 3.1 31.9 1.0
CE1 B:HIS620 3.1 32.2 1.0
CD2 A:HIS620 3.2 32.5 1.0
CD2 B:HIS620 3.2 33.1 1.0
ND1 A:HIS620 4.2 30.0 1.0
ND1 B:HIS620 4.3 27.7 1.0
CG A:HIS620 4.3 30.0 1.0
CG B:HIS620 4.3 31.7 1.0

Reference:

R.Wiener, Y.Haitin, L.Shamgar, M.C.Fernandez-Alonso, A.Martos, O.Chomsky-Hecht, G.Rivas, B.Attali, J.A.Hirsch. The KCNQ1 (KV7.1) Cooh Terminus, A Multitiered Scaffold For Subunit Assembly and Protein Interaction. J.Biol.Chem. V. 283 5815 2008.
ISSN: ISSN 0021-9258
PubMed: 18165683
DOI: 10.1074/JBC.M707541200
Page generated: Fri Sep 25 08:19:56 2020
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