Atomistry » Zinc » PDB 2afo-2aqr » 2aqn
Atomistry »
  Zinc »
    PDB 2afo-2aqr »
      2aqn »

Zinc in PDB 2aqn: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis

Enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis, PDB code: 2aqn was solved by M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.40
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.791, 64.592, 82.730, 90.00, 125.93, 90.00
R / Rfree (%) 12.9 / 19

Other elements in 2aqn:

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis also contains other interesting chemical elements:

Copper (Cu) 5 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis (pdb code 2aqn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis, PDB code: 2aqn:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2aqn

Go back to Zinc Binding Sites List in 2aqn
Zinc binding site 1 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:15.7
occ:1.00
OD1 A:ASP125 1.9 16.5 1.0
ND1 A:HIS122 2.0 16.4 1.0
ND1 A:HIS104 2.0 16.3 1.0
ND1 A:HIS113 2.1 15.6 1.0
CG A:ASP125 2.7 15.6 1.0
OD2 A:ASP125 2.8 16.8 1.0
CE1 A:HIS104 2.9 20.5 1.0
CE1 A:HIS113 3.0 16.9 1.0
CE1 A:HIS122 3.0 16.3 1.0
CG A:HIS122 3.1 15.9 1.0
CG A:HIS104 3.1 16.8 1.0
CG A:HIS113 3.1 16.2 1.0
CB A:HIS122 3.5 16.1 1.0
CB A:HIS104 3.5 16.7 1.0
CB A:HIS113 3.6 16.9 1.0
CA A:HIS113 3.7 16.1 1.0
NE2 A:HIS113 4.1 16.9 1.0
NE2 A:HIS104 4.1 18.4 1.0
NE2 A:HIS122 4.1 17.6 1.0
CB A:ASP125 4.1 15.4 1.0
CD2 A:HIS122 4.2 16.9 1.0
CD2 A:HIS104 4.2 20.9 1.0
CD2 A:HIS113 4.2 16.4 1.0
CD2 A:LEU173 4.5 25.1 1.0
N A:GLY114 4.6 15.7 1.0
CA A:ASP125 4.7 15.6 1.0
N A:HIS113 4.7 16.1 1.0
C A:HIS113 4.7 17.5 1.0
CA A:HIS122 4.8 16.1 1.0
O A:GLN112 4.9 18.1 1.0
N A:ASP125 4.9 16.0 1.0
CD2 A:HIS79 4.9 16.1 1.0
N A:HIS122 4.9 16.9 1.0

Zinc binding site 2 out of 3 in 2aqn

Go back to Zinc Binding Sites List in 2aqn
Zinc binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:16.4
occ:0.93
OD1 B:ASP125 1.9 18.3 1.0
ND1 B:HIS122 2.0 18.3 1.0
ND1 B:HIS113 2.1 18.9 1.0
ND1 B:HIS104 2.1 18.8 1.0
CG B:ASP125 2.7 17.5 1.0
OD2 B:ASP125 2.8 17.8 1.0
CE1 B:HIS113 2.9 18.0 1.0
CE1 B:HIS104 3.0 21.0 1.0
CE1 B:HIS122 3.0 20.3 1.0
CG B:HIS122 3.1 18.5 1.0
CG B:HIS104 3.2 19.2 1.0
CG B:HIS113 3.2 18.7 1.0
CB B:HIS122 3.4 19.4 1.0
CB B:HIS104 3.5 20.8 1.0
CB B:HIS113 3.7 18.4 1.0
CA B:HIS113 3.8 18.3 1.0
CB B:ASP125 4.1 16.9 1.0
NE2 B:HIS104 4.1 21.6 1.0
NE2 B:HIS113 4.1 18.0 1.0
NE2 B:HIS122 4.2 20.6 1.0
CD2 B:HIS122 4.2 19.6 1.0
CD2 B:HIS104 4.3 21.9 1.0
CD2 B:HIS113 4.3 17.7 1.0
CD2 B:LEU173 4.6 25.0 1.0
CA B:ASP125 4.6 18.0 1.0
N B:GLY114 4.6 16.8 1.0
CA B:HIS122 4.7 19.2 1.0
N B:HIS113 4.7 19.3 1.0
C B:HIS113 4.7 17.3 1.0
N B:ASP125 4.8 17.6 1.0
N B:HIS122 4.9 19.3 1.0
O B:GLN112 4.9 18.9 1.0
CD2 B:HIS79 4.9 16.0 1.0

Zinc binding site 3 out of 3 in 2aqn

Go back to Zinc Binding Sites List in 2aqn
Zinc binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn201

b:14.8
occ:1.00
OD1 C:ASP125 1.9 15.3 1.0
ND1 C:HIS104 2.0 15.8 1.0
ND1 C:HIS113 2.0 14.6 1.0
ND1 C:HIS122 2.1 15.3 1.0
CG C:ASP125 2.7 15.2 1.0
OD2 C:ASP125 2.8 15.5 1.0
CE1 C:HIS104 2.8 17.2 1.0
CE1 C:HIS113 2.9 15.1 1.0
CE1 C:HIS122 3.0 14.7 1.0
CG C:HIS113 3.1 13.8 1.0
CG C:HIS104 3.1 16.3 1.0
CG C:HIS122 3.1 14.7 1.0
CB C:HIS122 3.5 15.4 1.0
CB C:HIS104 3.5 17.8 1.0
CB C:HIS113 3.6 14.6 1.0
CA C:HIS113 3.8 14.8 1.0
NE2 C:HIS104 4.0 17.9 1.0
NE2 C:HIS113 4.1 14.4 1.0
CB C:ASP125 4.1 14.7 1.0
NE2 C:HIS122 4.2 16.3 1.0
CD2 C:HIS104 4.2 19.8 1.0
CD2 C:HIS113 4.2 14.5 1.0
CD2 C:HIS122 4.3 16.2 1.0
CD2 C:LEU173 4.4 27.2 1.0
CA C:ASP125 4.7 14.0 1.0
N C:HIS113 4.7 16.7 1.0
N C:GLY114 4.7 15.0 1.0
CA C:HIS122 4.8 14.7 1.0
C C:HIS113 4.8 15.4 1.0
CD2 C:HIS79 4.8 14.1 1.0
N C:HIS122 4.9 15.8 1.0
N C:ASP125 4.9 14.4 1.0
O C:GLN112 4.9 18.2 1.0
CG C:HIS79 5.0 15.2 1.0

Reference:

M.Didonato, C.J.Kassmann, C.K.Bruns, D.E.Cabelli, Z.Cao, L.B.Tabatabai, J.S.Kroll, E.D.Getzoff. Cu/Zn Superoxide Dismutase From Neisseria Meningitidis To Be Published.
Page generated: Wed Oct 16 21:44:46 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy