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Zinc in PDB 4xag: Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function

Protein crystallography data

The structure of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function, PDB code: 4xag was solved by C.J.Jackson, E.Campbell, M.Kaltenbach, N.Tokuriki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.41 / 1.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 85.886, 86.304, 88.583, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 20.2

Other elements in 4xag:

The structure of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function also contains other interesting chemical elements:

Arsenic (As) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function (pdb code 4xag). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function, PDB code: 4xag:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 4xag

Go back to Zinc Binding Sites List in 4xag
Zinc binding site 1 out of 4 in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2401

b:10.9
occ:1.00
O A:HOH2705 2.0 14.8 1.0
NE2 A:HIS57 2.1 9.0 1.0
NE2 A:HIS55 2.1 10.5 1.0
OD1 A:ASP301 2.1 11.1 1.0
OQ2 A:KCX169 2.2 10.3 1.0
CE1 A:HIS57 3.0 10.1 1.0
CD2 A:HIS55 3.0 9.4 1.0
CX A:KCX169 3.0 14.5 1.0
CG A:ASP301 3.1 10.8 1.0
CD2 A:HIS57 3.1 8.1 1.0
CE1 A:HIS55 3.2 11.3 1.0
ZN A:ZN2402 3.3 13.7 1.0
OQ1 A:KCX169 3.4 11.5 1.0
OD2 A:ASP301 3.4 11.4 1.0
O A:HOH2639 3.6 19.8 1.0
O2 A:MPD2404 3.9 20.3 1.0
CM A:MPD2404 4.0 23.2 1.0
CG2 A:VAL101 4.1 9.0 1.0
C3 A:MPD2404 4.1 28.1 1.0
NZ A:KCX169 4.1 12.3 1.0
ND1 A:HIS57 4.1 10.7 1.0
CG A:HIS57 4.2 8.0 1.0
CG A:HIS55 4.2 8.9 1.0
ND1 A:HIS55 4.3 9.4 1.0
CE1 A:HIS230 4.3 13.3 1.0
C2 A:MPD2404 4.3 27.1 1.0
NE2 A:HIS230 4.3 10.0 1.0
CB A:ASP301 4.4 10.3 1.0
CA A:ASP301 4.9 9.7 1.0

Zinc binding site 2 out of 4 in 4xag

Go back to Zinc Binding Sites List in 4xag
Zinc binding site 2 out of 4 in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2402

b:13.7
occ:1.00
ND1 A:HIS201 2.0 11.9 1.0
OQ1 A:KCX169 2.0 11.5 1.0
NE2 A:HIS230 2.0 10.0 1.0
O A:HOH2705 2.1 14.8 1.0
CE1 A:HIS201 2.9 14.6 1.0
CX A:KCX169 2.9 14.5 1.0
CE1 A:HIS230 3.0 13.3 1.0
CD2 A:HIS230 3.1 12.7 1.0
CG A:HIS201 3.1 14.4 1.0
OQ2 A:KCX169 3.2 10.3 1.0
ZN A:ZN2401 3.3 10.9 1.0
O A:HOH2639 3.3 19.8 1.0
CB A:HIS201 3.6 11.8 1.0
O2 A:MPD2404 3.6 20.3 1.0
CE1 A:HIS55 3.8 11.3 1.0
NE2 A:HIS55 3.8 10.5 1.0
NE2 A:HIS201 4.0 17.0 1.0
NE1 A:TRP131 4.1 17.5 1.0
OD2 A:ASP301 4.1 11.4 1.0
NZ A:KCX169 4.1 12.3 1.0
ND1 A:HIS230 4.1 13.9 1.0
CD2 A:HIS201 4.1 15.4 1.0
CG A:HIS230 4.2 10.0 1.0
CA A:HIS201 4.2 12.9 1.0
OD1 A:ASP301 4.6 11.1 1.0
CE A:KCX169 4.6 12.7 1.0
CG A:ASP301 4.7 10.8 1.0
CD1 A:TRP131 4.8 14.2 1.0
C2 A:MPD2404 4.8 27.1 1.0
CM A:MPD2404 5.0 23.2 1.0
ND1 A:HIS55 5.0 9.4 1.0

Zinc binding site 3 out of 4 in 4xag

Go back to Zinc Binding Sites List in 4xag
Zinc binding site 3 out of 4 in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn402

b:13.8
occ:1.00
O1 G:CAC401 2.0 10.5 0.7
NE2 G:HIS55 2.1 12.6 1.0
NE2 G:HIS57 2.1 11.4 1.0
OQ2 G:KCX169 2.2 14.8 1.0
OD1 G:ASP301 2.2 13.1 1.0
CD2 G:HIS55 3.0 13.2 1.0
CE1 G:HIS57 3.0 14.3 1.0
CX G:KCX169 3.0 14.5 1.0
CG G:ASP301 3.1 16.2 1.0
CE1 G:HIS55 3.1 15.3 1.0
CD2 G:HIS57 3.1 11.7 1.0
AS G:CAC401 3.3 57.7 0.7
ZN G:ZN403 3.3 16.6 1.0
OQ1 G:KCX169 3.4 12.9 1.0
OD2 G:ASP301 3.4 15.8 1.0
C2 G:CAC401 3.8 24.7 0.7
NZ G:KCX169 4.1 14.6 1.0
CG2 G:VAL101 4.1 8.8 1.0
CG G:HIS55 4.2 10.3 1.0
ND1 G:HIS57 4.2 12.8 1.0
CE1 G:HIS230 4.2 15.3 1.0
ND1 G:HIS55 4.2 12.8 1.0
NE2 G:HIS230 4.2 13.2 1.0
CG G:HIS57 4.3 12.6 1.0
CB G:ASP301 4.4 12.0 1.0
O2 G:CAC401 4.5 47.7 0.7
C1 G:CAC401 4.6 39.4 0.7
CA G:ASP301 4.9 11.6 1.0

Zinc binding site 4 out of 4 in 4xag

Go back to Zinc Binding Sites List in 4xag
Zinc binding site 4 out of 4 in the Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cycles of Destabilization and Repair Underlie the Evolution of New Enzyme Function within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Zn403

b:16.6
occ:1.00
ND1 G:HIS201 1.9 14.7 1.0
OQ1 G:KCX169 1.9 12.9 1.0
NE2 G:HIS230 2.0 13.2 1.0
O1 G:CAC401 2.0 10.5 0.7
CE1 G:HIS201 2.8 21.4 1.0
CX G:KCX169 2.9 14.5 1.0
CD2 G:HIS230 3.0 20.2 1.0
CE1 G:HIS230 3.0 15.3 1.0
O2 G:CAC401 3.1 47.7 0.7
CG G:HIS201 3.1 15.5 1.0
O G:HOH699 3.1 31.3 1.0
AS G:CAC401 3.2 57.7 0.7
OQ2 G:KCX169 3.2 14.8 1.0
ZN G:ZN402 3.3 13.8 1.0
CB G:HIS201 3.6 14.2 1.0
CE1 G:HIS55 3.8 15.3 1.0
NE2 G:HIS55 3.8 12.6 1.0
NE2 G:HIS201 4.0 19.3 1.0
ND1 G:HIS230 4.1 14.8 1.0
CD2 G:HIS201 4.1 22.5 1.0
CG G:HIS230 4.1 14.6 1.0
NE1 G:TRP131 4.1 14.2 1.0
NZ G:KCX169 4.1 14.6 1.0
OD2 G:ASP301 4.2 15.8 1.0
CA G:HIS201 4.4 13.0 1.0
C1 G:CAC401 4.5 39.4 0.7
CE G:KCX169 4.6 13.5 1.0
C2 G:CAC401 4.7 24.7 0.7
OD1 G:ASP301 4.7 13.1 1.0
CG G:ASP301 4.8 16.2 1.0
CD1 G:TRP131 4.8 15.1 1.0
O G:HOH686 4.9 31.5 1.0
O G:HOH688 5.0 41.0 1.0

Reference:

E.Campbell, M.Kaltenbach, G.J.Correy, P.D.Carr, B.T.Porebski, E.K.Livingstone, L.Afriat-Jurnou, A.M.Buckle, M.Weik, F.Hollfelder, N.Tokuriki, C.J.Jackson. The Role of Protein Dynamics in the Evolution of New Enzyme Function. Nat.Chem.Biol. V. 12 944 2016.
ISSN: ESSN 1552-4469
PubMed: 27618189
DOI: 10.1038/NCHEMBIO.2175
Page generated: Wed Dec 16 05:54:05 2020

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