Zinc in PDB 3gj9: Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3

The structure of Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3, PDB code: 3gj9 was solved by Y.Shen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.27 / 2.80
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	86.457, 86.457, 101.517, 90.00, 90.00, 90.00
R / Rfree (%)	24.7 / 27

The structure of Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3 also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Zinc atom in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3 (pdb code 3gj9). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3, PDB code: 3gj9:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3


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 Tip-1 in Complex with C-Terminal of KIR2.3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn125 b:0.5 occ:1.00 OE2 A:GLU103 2.0 77.5 1.0 ND1 A:HIS19 2.7 66.9 1.0 CB A:HIS19 2.9 56.5 1.0 CG A:HIS19 3.2 64.2 1.0 CD A:GLU103 3.3 76.7 1.0 CE1 A:HIS19 3.9 65.7 1.0 CG A:GLU103 4.1 72.3 1.0 OE1 A:GLU103 4.2 81.1 1.0 CA A:HIS19 4.2 52.3 1.0 CD2 A:HIS19 4.4 65.8 1.0 C A:HIS19 4.7 50.9 1.0 CG2 A:VAL104 4.7 46.6 1.0 O A:LYS20 4.7 51.6 1.0 NE2 A:HIS19 4.8 65.0 1.0 O A:GLU103 4.9 54.4 1.0 O A:HOH151 4.9 57.3 1.0

Zinc binding site 2 out of 4 in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3


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 Tip-1 in Complex with C-Terminal of KIR2.3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn125 b:0.8 occ:1.00 OE2 B:GLU103 2.1 79.3 1.0 ND1 B:HIS19 2.9 66.5 1.0 CD B:GLU103 3.4 78.5 1.0 CB B:HIS19 3.4 57.6 1.0 O B:HOH162 3.4 53.5 1.0 CG B:HIS19 3.5 64.6 1.0 CE1 B:HIS19 4.0 65.7 1.0 OE1 B:GLU103 4.1 82.2 1.0 CG B:GLU103 4.4 74.5 1.0 CA B:HIS19 4.7 53.6 1.0 CD2 B:HIS19 4.7 66.1 1.0 CG2 B:VAL104 4.9 48.5 1.0 NE2 B:HIS19 5.0 66.0 1.0

Zinc binding site 3 out of 4 in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn126 b:59.0 occ:1.00 OE2 B:GLU62 2.0 32.5 1.0 OE2 B:GLU67 2.0 52.8 1.0 O B:HOH164 2.6 51.7 1.0 CD B:GLU62 2.7 37.1 1.0 OE1 B:GLU62 2.8 38.2 1.0 O B:HOH135 2.9 51.0 1.0 CD B:GLU67 2.9 49.9 1.0 O B:HOH137 3.1 32.6 1.0 OE1 B:GLU67 3.2 49.7 1.0 CG B:GLU62 4.2 39.6 1.0 CG B:GLU67 4.3 46.6 1.0 N B:GLY63 4.8 44.5 1.0

Zinc binding site 4 out of 4 in the Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Tip-1 in Complex with C-Terminal of KIR2.3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn127 b:52.7 occ:1.00 OE2 B:GLU17 1.7 66.0 1.0 OE2 A:GLU62 1.8 30.1 1.0 OE2 A:GLU67 2.1 50.0 1.0 CD B:GLU17 2.3 64.0 1.0 O A:HOH128 2.3 43.7 1.0 OE1 B:GLU17 2.3 64.7 1.0 CD A:GLU62 2.6 33.6 1.0 O B:HOH134 2.7 62.7 1.0 OE1 A:GLU62 2.8 35.8 1.0 CD A:GLU67 3.0 48.0 1.0 O B:HOH138 3.1 35.7 1.0 OE1 A:GLU67 3.2 46.8 1.0 CG B:GLU17 3.8 60.0 1.0 NH1 B:ARG106 4.0 48.8 1.0 CG A:GLU62 4.1 35.7 1.0 CG A:GLU67 4.4 44.1 1.0 CB B:GLU17 4.7 57.1 1.0 NE2 B:HIS19 4.8 66.0 1.0 N A:GLY63 4.9 38.9 1.0

X.Yan, H.Zhou, J.Zhang, C.Shi, X.Xie, Y.Wu, C.Tian, Y.Shen, J.Long. Molecular Mechanism of Inward Rectifier Potassium Channel 2.3 Regulation By Tax-Interacting Protein-1 J.Mol.Biol. V. 392 967 2009.
ISSN: ISSN 0022-2836
PubMed: 19635485
DOI: 10.1016/J.JMB.2009.07.060