Zinc in PDB 4htm: Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2

The structure of Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2, PDB code: 4htm was solved by Q.Luo, K.Viste, J.C.Urday-Zaa, G.S.Kumar, W.-W.Tsai, A.Talai, K.Mayo, M.Montminy, I.Radhakrishnan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.41 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	21.481, 57.631, 23.065, 90.00, 94.58, 90.00
R / Rfree (%)	24.8 / 28.4

The binding sites of Zinc atom in the Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2 (pdb code 4htm). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2, PDB code: 4htm:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:27.9 occ:1.00 OE2 A:GLU25 1.8 20.3 1.0 O A:HOH216 2.4 19.4 1.0 CD A:GLU25 2.7 19.1 1.0 OE1 A:GLU25 3.0 19.5 1.0 CG A:GLU25 4.1 17.9 1.0 CG2 A:THR21 4.4 17.4 1.0

Zinc binding site 2 out of 3 in the Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:12.8 occ:0.50 OE1 A:GLU26 1.9 25.0 1.0 OD2 A:ASP30 2.2 23.1 1.0 CG A:ASP30 3.0 21.5 1.0 CD A:GLU26 3.0 25.2 1.0 OD1 A:ASP30 3.1 21.4 1.0 CG A:GLU26 3.4 25.6 1.0 OE2 A:GLU26 4.1 26.1 1.0 O A:GLU26 4.2 16.7 1.0 O A:HOH207 4.4 14.2 1.0 CB A:ASP30 4.4 21.3 1.0 C A:GLU26 4.8 17.3 1.0 CB A:GLU26 4.8 23.8 1.0

Zinc binding site 3 out of 3 in the Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Mechanism of Creb Recognition and Coactivation By the Creb Regulated Transcriptional Coactivator CRTC2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn103 b:18.2 occ:0.50 OE2 A:GLU19 2.2 24.4 1.0 OE1 A:GLU19 2.7 22.9 1.0 CD A:GLU19 2.8 22.5 1.0 O A:HOH202 4.1 16.1 1.0 CG A:GLU19 4.3 20.5 1.0 CG A:GLN15 4.4 20.2 1.0 NE2 A:GLN15 4.6 26.2 1.0

Q.Luo, K.Viste, J.C.Urday-Zaa, G.S.Kumar, W.-W.Tsai, A.Talai, K.Mayo, M.Montminy, I.Radhakrishnan. Protein Kinase N1, A Cell Inhibitor of Akt Kinase, Has A Central Role in Quality Control of Germinal Center Formation Proc.Natl.Acad.Sci.Usa 2012.
ISSN: ESSN 1091-6490