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Zinc in PDB 6sqc: Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076

Enzymatic activity of Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076

All present enzymatic activity of Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076:
2.3.1.48;

Protein crystallography data

The structure of Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076, PDB code: 6sqc was solved by V.Bauer, B.Schmidtgall, G.Gogl, J.Dolenc, J.Osz, C.Kostmann, A.Mitschler, A.Cousido-Siah, N.Rochel, G.Trave, B.Kieffer, V.Torbeev, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.72 / 2.28
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 103.180, 42.460, 113.790, 90.00, 101.13, 90.00
R / Rfree (%) 22.8 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076 (pdb code 6sqc). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076, PDB code: 6sqc:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 6sqc

Go back to Zinc Binding Sites List in 6sqc
Zinc binding site 1 out of 2 in the Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076


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 Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2202

b:61.5
occ:1.00
 O A:HIS1728 2.0 72.8 1.0
ND1 A:HIS1728 2.1 61.9 1.0
O A:HOH2418 2.2 53.0 1.0
O A:HOH2389 2.5 59.9 1.0
O A:HOH2429 2.7 47.1 1.0
CE1 A:HIS1728 3.1 57.8 1.0
C A:HIS1728 3.2 55.9 1.0
CG A:HIS1728 3.2 54.2 1.0
O A:HOH2369 3.3 44.3 1.0
CB A:HIS1728 3.5 44.3 1.0
O A:HOH2394 3.8 30.3 1.0
CA A:HIS1728 3.9 41.1 1.0
O A:HOH2431 4.2 48.1 1.0
NE2 A:HIS1728 4.2 57.5 1.0
N A:PRO1729 4.2 52.5 1.0
CD2 A:HIS1728 4.3 56.6 1.0
OD1 A:ASP1730 4.4 58.4 1.0
CA A:PRO1729 4.4 47.9 1.0
N A:HIS1728 4.5 47.8 1.0
C A:PRO1729 4.6 52.5 1.0
N A:ASP1730 4.9 50.3 1.0
O A:PRO1729 4.9 53.1 1.0

Zinc binding site 2 out of 2 in 6sqc

Go back to Zinc Binding Sites List in 6sqc
Zinc binding site 2 out of 2 in the Crystal Structure of Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076


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 Complex Between Nuclear Coactivator Binding Domain of Cbp and [1040-1086]Actr Containing Alpha-Methylated LEU1055 and LEU1076 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2203

b:60.7
occ:1.00
 NZ A:LYS2075 2.1 84.5 1.0
O A:HOH2334 2.2 55.0 1.0
N A:MET1689 2.3 69.8 0.7
O A:MET1689 2.4 65.2 0.3
CA A:MET1689 2.4 67.6 0.7
O A:MET1689 2.4 65.4 0.7
OD1 A:ASP1744 2.4 71.0 1.0
CA A:MET1689 2.5 67.4 0.3
OD2 A:ASP1744 2.5 68.3 1.0
C A:MET1689 2.7 66.1 0.7
C A:MET1689 2.8 65.6 0.3
CG A:ASP1744 2.8 63.7 1.0
N A:MET1689 3.0 67.3 0.3
NE2 B:GLN1051 3.4 84.9 1.0
CE A:LYS2075 3.6 69.3 1.0
CB A:MET1689 3.8 68.8 0.3
SD A:MET1689 3.9 64.7 0.3
CB A:MET1689 3.9 68.3 0.7
N A:LYS1690 4.1 60.5 1.0
CB A:ASP1744 4.3 54.8 1.0
CG A:MET1689 4.3 69.3 0.3
CD A:LYS2075 4.5 64.9 1.0
CD B:GLN1051 4.5 80.7 1.0
O A:THR1742 4.5 46.4 1.0
CG A:MET1689 4.7 68.1 0.7
CG A:LYS2075 4.7 56.5 1.0
OG1 A:THR1742 4.8 45.2 1.0
OE1 B:GLN1051 4.8 83.0 1.0
CA A:ASP1744 4.8 45.7 1.0
O A:GLY1743 4.9 60.8 1.0

Reference:

V.Bauer, B.Schmidtgall, G.Gogl, J.Dolenc, J.Osz, C.Kostmann, A.Mitschler, A.Cousido-Siah, N.Rochel, G.Trave, B.Kieffer, V.Torbeev. Enhancing Binding Affinity of An Intrinsically Disordered Protein By A-Methylation of Key Amino Acid Residues To Be Published.
Page generated: Tue Oct 29 07:38:15 2024

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