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Zinc in PDB 2aqr: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant

Enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant, PDB code: 2aqr 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) 29.47 / 1.75
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.840, 65.052, 77.443, 90.00, 121.02, 90.00
R / Rfree (%) 16.9 / 19.7

Other elements in 2aqr:

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant 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 K91Q Mutant (pdb code 2aqr). 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 K91Q Mutant, PDB code: 2aqr:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 2aqr

Go back to Zinc Binding Sites List in 2aqr
Zinc binding site 1 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


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 K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:12.4
occ:1.00
OD1 A:ASP125 1.9 11.0 1.0
ND1 A:HIS104 2.0 10.4 1.0
ND1 A:HIS113 2.1 9.5 1.0
ND1 A:HIS122 2.1 11.1 1.0
CG A:ASP125 2.8 8.9 1.0
CE1 A:HIS113 2.9 10.6 1.0
CE1 A:HIS104 2.9 11.5 1.0
OD2 A:ASP125 3.0 11.4 1.0
CE1 A:HIS122 3.1 12.5 1.0
CG A:HIS122 3.1 12.4 1.0
CG A:HIS104 3.1 11.9 1.0
CG A:HIS113 3.2 12.2 1.0
CB A:HIS122 3.4 11.7 1.0
CB A:HIS104 3.5 10.5 1.0
CB A:HIS113 3.6 12.1 1.0
CA A:HIS113 3.8 11.1 1.0
NE2 A:HIS104 4.1 12.2 1.0
NE2 A:HIS113 4.1 11.5 1.0
NE2 A:HIS122 4.2 12.0 1.0
CD2 A:HIS104 4.2 11.1 1.0
CB A:ASP125 4.2 10.5 1.0
CD2 A:HIS122 4.2 13.1 1.0
CD2 A:HIS113 4.2 10.2 1.0
CD2 A:LEU173 4.6 16.6 1.0
N A:GLY114 4.7 11.9 1.0
CA A:ASP125 4.7 10.2 1.0
CA A:HIS122 4.7 11.8 1.0
C A:HIS113 4.8 13.3 1.0
N A:HIS113 4.8 13.4 1.0
CD2 A:HIS79 4.8 11.0 1.0
N A:ASP125 4.8 10.6 1.0
N A:HIS122 4.8 13.0 1.0
O A:GLN112 4.9 12.8 1.0

Zinc binding site 2 out of 3 in 2aqr

Go back to Zinc Binding Sites List in 2aqr
Zinc binding site 2 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


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 K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:12.8
occ:1.00
OD1 B:ASP125 1.9 9.6 1.0
ND1 B:HIS104 2.1 11.8 1.0
ND1 B:HIS113 2.1 11.3 1.0
ND1 B:HIS122 2.1 12.4 1.0
CG B:ASP125 2.7 9.7 1.0
OD2 B:ASP125 2.8 9.5 1.0
CE1 B:HIS113 2.9 11.5 1.0
CE1 B:HIS104 3.0 14.8 1.0
CG B:HIS122 3.1 13.8 1.0
CE1 B:HIS122 3.1 15.2 1.0
CG B:HIS104 3.1 14.9 1.0
CG B:HIS113 3.2 11.2 1.0
CB B:HIS122 3.4 11.8 1.0
CB B:HIS104 3.5 13.1 1.0
CB B:HIS113 3.6 12.2 1.0
CA B:HIS113 3.7 12.2 1.0
NE2 B:HIS113 4.1 11.2 1.0
CB B:ASP125 4.1 9.8 1.0
NE2 B:HIS104 4.1 14.5 1.0
CD2 B:HIS104 4.2 13.8 1.0
NE2 B:HIS122 4.2 14.9 1.0
CD2 B:HIS122 4.2 13.1 1.0
CD2 B:HIS113 4.2 12.1 1.0
CD2 B:LEU173 4.6 16.9 1.0
N B:GLY114 4.6 10.8 1.0
CA B:ASP125 4.7 10.2 1.0
CA B:HIS122 4.7 12.7 1.0
N B:HIS113 4.7 12.8 1.0
C B:HIS113 4.7 12.9 1.0
N B:HIS122 4.8 13.1 1.0
N B:ASP125 4.8 10.3 1.0
CD2 B:HIS79 4.9 10.9 1.0
O B:GLN112 4.9 13.3 1.0

Zinc binding site 3 out of 3 in 2aqr

Go back to Zinc Binding Sites List in 2aqr
Zinc binding site 3 out of 3 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q Mutant


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 K91Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn201

b:11.9
occ:1.00
OD1 C:ASP125 2.0 8.3 1.0
ND1 C:HIS104 2.0 11.8 1.0
ND1 C:HIS113 2.1 9.1 1.0
ND1 C:HIS122 2.1 9.5 1.0
CG C:ASP125 2.7 9.6 1.0
OD2 C:ASP125 2.8 10.2 1.0
CE1 C:HIS104 2.9 12.1 1.0
CE1 C:HIS113 2.9 11.9 1.0
CE1 C:HIS122 3.1 11.5 1.0
CG C:HIS122 3.1 10.8 1.0
CG C:HIS104 3.1 13.2 1.0
CG C:HIS113 3.2 10.2 1.0
CB C:HIS122 3.4 12.1 1.0
CB C:HIS104 3.5 12.1 1.0
CB C:HIS113 3.6 10.3 1.0
CA C:HIS113 3.8 11.0 1.0
NE2 C:HIS104 4.1 12.5 1.0
NE2 C:HIS113 4.1 10.1 1.0
CB C:ASP125 4.1 9.7 1.0
CD2 C:HIS104 4.2 13.2 1.0
NE2 C:HIS122 4.2 11.2 1.0
CD2 C:HIS122 4.2 11.9 1.0
CD2 C:HIS113 4.3 10.5 1.0
CD2 C:LEU173 4.5 17.4 1.0
N C:GLY114 4.6 10.9 1.0
CA C:ASP125 4.7 9.9 1.0
CA C:HIS122 4.7 10.9 1.0
C C:HIS113 4.8 11.8 1.0
N C:HIS113 4.8 12.1 1.0
CD2 C:HIS79 4.8 8.4 1.0
N C:HIS122 4.8 12.7 1.0
N C:ASP125 4.8 9.6 1.0
O C:GLN112 4.8 11.4 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 K91Q Mutant To Be Published.
Page generated: Wed Dec 16 03:17:52 2020

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