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Copper in PDB 2aqt: Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant

Enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant

All present enzymatic activity of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant, PDB code: 2aqt 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) 49.44 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 98.209, 64.464, 85.051, 90.00, 128.33, 90.00
R / Rfree (%) 18.5 / 21.5

Other elements in 2aqt:

The structure of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant (pdb code 2aqt). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 5 binding sites of Copper where determined in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant, PDB code: 2aqt:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 2aqt

Go back to Copper Binding Sites List in 2aqt
Copper binding site 1 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu200

b:17.8
occ:1.00
ND1 C:HIS79 2.0 15.3 1.0
NE2 C:HIS160 2.1 13.2 1.0
NE2 C:HIS81 2.1 13.9 1.0
CD2 C:HIS160 2.9 15.6 1.0
CE1 C:HIS79 3.0 12.4 1.0
CG C:HIS79 3.0 13.4 1.0
CE1 C:HIS81 3.0 13.5 1.0
CD2 C:HIS81 3.1 12.7 1.0
CE1 C:HIS160 3.1 15.5 1.0
NE2 C:HIS104 3.3 16.0 1.0
CB C:HIS79 3.3 13.6 1.0
CD2 C:HIS104 3.7 15.3 1.0
CB C:MET158 3.8 14.2 1.0
O C:HOH628 4.0 26.3 1.0
CG C:MET158 4.1 14.3 1.0
CE1 C:HIS104 4.1 14.5 1.0
CG C:HIS160 4.1 15.1 1.0
NE2 C:HIS79 4.1 13.4 1.0
CD2 C:HIS79 4.2 13.2 1.0
ND1 C:HIS81 4.2 14.4 1.0
ND1 C:HIS160 4.2 14.5 1.0
CG C:HIS81 4.2 13.6 1.0
N C:HIS79 4.3 11.7 1.0
CA C:HIS79 4.3 14.5 1.0
CG C:HIS104 4.6 14.9 1.0
O C:HOH567 4.7 33.8 1.0
O C:HIS79 4.7 15.6 1.0
O C:MET158 4.7 15.9 1.0
C C:HIS79 4.7 13.2 1.0
ND1 C:HIS104 4.8 15.6 1.0

Copper binding site 2 out of 5 in 2aqt

Go back to Copper Binding Sites List in 2aqt
Copper binding site 2 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu301

b:15.3
occ:0.50
OE1 C:GLU73 2.0 14.9 1.0
ND1 C:HIS133 2.1 18.0 1.0
CD C:GLU73 2.7 15.1 1.0
OE2 C:GLU73 2.7 16.5 1.0
CE1 C:HIS133 3.0 18.4 1.0
CG C:HIS133 3.1 16.2 1.0
CB C:HIS133 3.4 15.9 1.0
CA C:HIS133 4.0 14.3 1.0
NE2 C:HIS133 4.1 16.6 1.0
CG C:GLU73 4.2 15.8 1.0
CD2 C:HIS133 4.2 16.2 1.0
O C:HOH432 4.4 15.1 1.0
N C:HIS133 4.7 13.8 1.0
CB C:GLU73 4.8 15.4 1.0
O B:HOH500 4.9 25.0 1.0

Copper binding site 3 out of 5 in 2aqt

Go back to Copper Binding Sites List in 2aqt
Copper binding site 3 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:22.3
occ:1.00
NE2 B:HIS81 2.1 15.5 1.0
ND1 B:HIS79 2.1 21.7 1.0
NE2 B:HIS160 2.1 19.8 1.0
CE1 B:HIS79 3.0 19.3 1.0
CE1 B:HIS81 3.0 16.7 1.0
CD2 B:HIS160 3.0 20.7 1.0
CD2 B:HIS81 3.1 16.6 1.0
CG B:HIS79 3.2 20.1 1.0
CE1 B:HIS160 3.2 19.9 1.0
NE2 B:HIS104 3.4 25.4 1.0
CB B:HIS79 3.6 19.2 1.0
CD2 B:HIS104 3.6 24.8 1.0
CB B:MET158 3.8 17.9 1.0
O B:HOH665 3.9 37.0 1.0
CG B:MET158 3.9 20.0 1.0
ND1 B:HIS81 4.1 17.1 1.0
NE2 B:HIS79 4.1 20.2 1.0
CG B:HIS160 4.2 19.5 1.0
CG B:HIS81 4.2 16.2 1.0
CD2 B:HIS79 4.2 19.0 1.0
ND1 B:HIS160 4.3 20.0 1.0
CE1 B:HIS104 4.3 25.0 1.0
N B:HIS79 4.3 16.7 1.0
CA B:HIS79 4.4 17.9 1.0
O B:HIS79 4.5 18.0 1.0
O B:MET158 4.6 19.9 1.0
CG B:HIS104 4.6 25.7 1.0
O B:HOH684 4.7 33.5 1.0
C B:HIS79 4.7 18.5 1.0
C B:MET158 4.9 18.8 1.0
CA B:MET158 4.9 18.4 1.0
ND1 B:HIS104 4.9 22.2 1.0

Copper binding site 4 out of 5 in 2aqt

Go back to Copper Binding Sites List in 2aqt
Copper binding site 4 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:20.5
occ:1.00
NE2 A:HIS81 2.0 16.7 1.0
NE2 A:HIS160 2.1 18.6 1.0
ND1 A:HIS79 2.1 17.1 1.0
CD2 A:HIS160 2.9 19.3 1.0
CE1 A:HIS81 3.0 19.4 1.0
CE1 A:HIS79 3.1 17.1 1.0
CD2 A:HIS81 3.1 17.4 1.0
CG A:HIS79 3.2 15.8 1.0
CE1 A:HIS160 3.2 20.5 1.0
NE2 A:HIS104 3.4 21.5 1.0
CB A:HIS79 3.5 15.8 1.0
CD2 A:HIS104 3.7 20.4 1.0
CB A:MET158 3.8 17.7 1.0
O A:HOH594 4.0 31.6 1.0
CG A:MET158 4.0 16.9 1.0
CG A:HIS160 4.1 18.8 1.0
ND1 A:HIS81 4.1 22.7 1.0
CG A:HIS81 4.2 18.1 1.0
ND1 A:HIS160 4.2 20.3 1.0
NE2 A:HIS79 4.2 16.6 1.0
CD2 A:HIS79 4.3 17.7 1.0
CE1 A:HIS104 4.3 21.7 1.0
N A:HIS79 4.4 16.5 1.0
CA A:HIS79 4.4 16.2 1.0
O A:HOH529 4.6 30.1 1.0
O A:HIS79 4.6 17.2 1.0
CG A:HIS104 4.7 20.5 1.0
O A:MET158 4.8 17.9 1.0
C A:HIS79 4.8 16.7 1.0
CA A:MET158 4.9 17.5 1.0
C A:MET158 5.0 16.9 1.0

Copper binding site 5 out of 5 in 2aqt

Go back to Copper Binding Sites List in 2aqt
Copper binding site 5 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Cu/Zn Superoxide Dismutase From Neisseria Meningitidis K91Q, K94Q Double Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu300

b:17.8
occ:1.00
OE1 B:GLU73 1.9 19.3 1.0
ND1 B:HIS133 2.0 19.1 1.0
OE1 A:GLU73 2.0 18.6 1.0
ND1 A:HIS133 2.1 19.4 1.0
CD B:GLU73 2.7 21.9 1.0
OE2 B:GLU73 2.8 23.6 1.0
CD A:GLU73 2.8 21.3 1.0
CE1 B:HIS133 2.8 22.7 1.0
OE2 A:GLU73 3.0 22.1 1.0
CG A:HIS133 3.0 18.1 1.0
CG B:HIS133 3.1 20.5 1.0
CE1 A:HIS133 3.1 19.0 1.0
CB A:HIS133 3.3 16.2 1.0
CB B:HIS133 3.5 17.5 1.0
CA A:HIS133 3.9 16.2 1.0
NE2 B:HIS133 4.0 23.0 1.0
CA B:HIS133 4.1 17.3 1.0
CD2 B:HIS133 4.1 21.6 1.0
CD2 A:HIS133 4.1 18.9 1.0
NE2 A:HIS133 4.2 18.5 1.0
CG B:GLU73 4.2 19.4 1.0
CG A:GLU73 4.3 20.0 1.0
O A:HOH502 4.3 22.1 1.0
O A:HOH407 4.5 17.6 1.0
N A:HIS133 4.7 16.0 1.0
CB B:GLU73 4.7 19.0 1.0
N B:HIS133 4.8 15.7 1.0
CB A:GLU73 4.9 19.2 1.0
O A:HOH537 4.9 26.0 1.0
O C:HOH428 5.0 21.3 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, K94Q Double Mutant To Be Published.
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