Atomistry » Zinc » PDB 6r52-6rd7 » 6r7n
Atomistry »
  Zinc »
    PDB 6r52-6rd7 »
      6r7n »

Zinc in PDB 6r7n: Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome (pdb code 6r7n). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome, PDB code: 6r7n:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 6r7n

Go back to Zinc Binding Sites List in 6r7n
Zinc binding site 1 out of 3 in the Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Zn201

b:0.4
occ:1.00
O R:LEU52 2.1 0.0 1.0
OD1 R:ASP51 3.3 0.9 1.0
C R:LEU52 3.3 0.7 1.0
OD2 R:ASP51 3.3 0.9 1.0
CG R:ASP51 3.6 0.2 1.0
CA R:LEU52 4.0 0.3 1.0
CB R:LEU52 4.1 0.1 1.0
N R:LEU52 4.1 0.4 1.0
N R:CYS53 4.3 0.1 1.0
O R:CYS53 4.5 0.4 1.0
CA R:CYS53 4.6 0.1 1.0
C R:CYS53 4.7 0.2 1.0
C R:ASP51 5.0 0.7 1.0

Zinc binding site 2 out of 3 in 6r7n

Go back to Zinc Binding Sites List in 6r7n
Zinc binding site 2 out of 3 in the Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Zn202

b:0.9
occ:1.00
N R:CYS68 2.2 0.6 1.0
CA R:GLU67 2.5 0.1 1.0
CD1 R:ILE49 2.5 0.8 1.0
CG2 R:VAL70 2.5 0.2 1.0
C R:GLU67 2.7 0.9 1.0
CB R:VAL70 2.9 0.9 1.0
O R:GLU66 3.2 0.5 1.0
N R:GLU67 3.3 0.5 1.0
CA R:CYS68 3.3 0.8 1.0
CG1 R:ILE49 3.4 0.0 1.0
N R:THR69 3.5 0.8 1.0
C R:GLU66 3.5 0.4 1.0
N R:VAL70 3.6 0.6 1.0
CB R:GLU67 3.7 0.3 1.0
CB R:CYS68 3.7 0.5 1.0
C R:CYS68 3.8 0.3 1.0
CA R:VAL70 3.8 0.8 1.0
C R:THR69 3.9 0.9 1.0
O R:GLU67 3.9 0.8 1.0
CG R:GLU67 3.9 0.1 1.0
O R:ILE49 4.1 0.7 1.0
CG1 R:VAL70 4.1 0.5 1.0
OE1 B:GLN297 4.2 0.8 1.0
CA R:THR69 4.3 0.1 1.0
O R:THR69 4.4 0.6 1.0
CA R:ILE49 4.6 0.7 1.0
CB R:ILE49 4.6 0.7 1.0
C R:ILE49 4.8 0.3 1.0
O R:CYS68 4.9 0.5 1.0
CA R:GLU66 4.9 0.4 1.0

Zinc binding site 3 out of 3 in 6r7n

Go back to Zinc Binding Sites List in 6r7n
Zinc binding site 3 out of 3 in the Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structural Basis of Cullin-2 Ring E3 Ligase Regulation By the COP9 Signalosome within 5.0Å range:
probe atom residue distance (Å) B Occ
R:Zn203

b:0.4
occ:1.00
CB R:GLU55 2.6 0.7 1.0
CG R:GLU55 2.6 0.4 1.0
CB R:PHE81 2.6 0.5 1.0
CD2 R:PHE81 2.9 0.2 1.0
CA R:GLU55 3.1 0.9 1.0
CG R:PHE81 3.1 0.8 1.0
O R:GLU55 3.5 0.8 1.0
CA R:PHE81 3.6 0.6 1.0
N R:PHE81 3.6 0.5 1.0
N R:HIS82 3.7 0.3 1.0
ND1 R:HIS82 3.7 1.0 1.0
C R:GLU55 3.8 0.0 1.0
CD R:GLU55 4.1 0.8 1.0
C R:PHE81 4.1 0.8 1.0
CE2 R:PHE81 4.2 0.7 1.0
N R:GLU55 4.4 0.3 1.0
CD1 R:PHE81 4.5 0.8 1.0
CE1 R:HIS82 4.5 0.2 1.0
CG R:HIS82 4.7 0.6 1.0
C R:HIS80 4.7 1.0 1.0
OE2 R:GLU55 4.7 0.8 1.0
CB R:HIS82 4.8 1.0 1.0
CA R:HIS82 4.8 0.9 1.0
OE1 R:GLU55 4.9 0.2 1.0

Reference:

S.V.Faull, A.M.C.Lau, C.Martens, Z.Ahdash, K.Hansen, H.Yebenes, C.Schmidt, F.Beuron, N.B.Cronin, E.P.Morris, A.Politis. Structural Basis of Cullin 2 Ring E3 Ligase Regulation By the COP9 Signalosome. Nat Commun V. 10 3814 2019.
ISSN: ESSN 2041-1723
PubMed: 31444342
DOI: 10.1038/S41467-019-11772-Y
Page generated: Tue Oct 29 06:06:02 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy