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Copper in PDB 2aqq: Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant

Enzymatic activity of Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant

All present enzymatic activity of Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant:
1.15.1.1;

Protein crystallography data

The structure of Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant, PDB code: 2aqq 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) 29.14 / 1.65
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.661, 64.685, 82.843, 90.00, 125.91, 90.00
R / Rfree (%) 17.2 / 19.6

Other elements in 2aqq:

The structure of Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant also contains other interesting chemical elements:

Zinc (Zn) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E Mutant (pdb code 2aqq). 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant, PDB code: 2aqq:
Jump to Copper binding site number: 1; 2; 3; 4; 5;

Copper binding site 1 out of 5 in 2aqq

Go back to Copper Binding Sites List in 2aqq
Copper binding site 1 out of 5 in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:14.4
occ:1.00
 NE2 A:HIS81 2.0 10.5 1.0
ND1 A:HIS79 2.0 11.3 1.0
NE2 A:HIS160 2.0 12.2 1.0
CD2 A:HIS160 2.9 10.4 1.0
CE1 A:HIS79 2.9 11.1 1.0
CE1 A:HIS81 3.0 13.1 1.0
CD2 A:HIS81 3.0 12.4 1.0
CG A:HIS79 3.1 10.8 1.0
CE1 A:HIS160 3.1 12.1 1.0
NE2 A:HIS104 3.3 13.6 1.0
CB A:HIS79 3.4 11.9 1.0
CD2 A:HIS104 3.6 13.5 1.0
CB A:MET158 3.8 10.1 1.0
O A:HOH483 4.0 17.8 1.0
CG A:MET158 4.0 10.3 1.0
NE2 A:HIS79 4.1 9.9 1.0
CE1 A:HIS104 4.1 12.6 1.0
ND1 A:HIS81 4.1 10.4 1.0
CG A:HIS160 4.1 11.1 1.0
CG A:HIS81 4.1 9.1 1.0
O A:HOH495 4.1 16.6 1.0
CD2 A:HIS79 4.2 10.8 1.0
ND1 A:HIS160 4.2 11.4 1.0
N A:HIS79 4.3 11.5 1.0
CA A:HIS79 4.4 10.2 1.0
CG A:HIS104 4.5 12.9 1.0
O A:HIS79 4.6 11.6 1.0
C A:HIS79 4.7 11.7 1.0
ND1 A:HIS104 4.7 13.3 1.0
O A:MET158 4.7 12.2 1.0
CA A:MET158 5.0 11.7 1.0
C A:MET158 5.0 10.4 1.0

Copper binding site 2 out of 5 in 2aqq

Go back to Copper Binding Sites List in 2aqq
Copper binding site 2 out of 5 in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu250

b:19.6
occ:1.00
 OE1 A:GLU73 1.9 21.3 1.0
OE1 B:GLU73 2.0 21.6 1.0
ND1 B:HIS133 2.0 18.1 1.0
ND1 A:HIS133 2.1 20.0 1.0
CD A:GLU73 2.6 15.7 1.0
OE2 A:GLU73 2.7 21.7 1.0
CD B:GLU73 2.8 20.6 1.0
CE1 B:HIS133 2.9 21.0 1.0
OE2 B:GLU73 3.0 26.0 1.0
CE1 A:HIS133 3.0 18.2 1.0
CG B:HIS133 3.0 18.5 1.0
CG A:HIS133 3.1 17.4 1.0
CB A:HIS133 3.4 15.7 1.0
CB B:HIS133 3.4 16.4 1.0
CA B:HIS133 4.0 16.3 1.0
CG A:GLU73 4.0 20.2 1.0
NE2 B:HIS133 4.0 20.5 1.0
CA A:HIS133 4.1 16.8 1.0
CD2 B:HIS133 4.1 18.5 1.0
NE2 A:HIS133 4.1 20.9 1.0
CD2 A:HIS133 4.2 19.0 1.0
CG B:GLU73 4.2 20.4 1.0
O A:HOH464 4.3 16.6 1.0
O A:HOH578 4.6 32.7 1.0
O B:HOH682 4.7 30.5 1.0
CB B:GLU73 4.7 15.7 1.0
N A:HIS133 4.8 15.6 1.0
N B:HIS133 4.8 15.9 1.0
O A:HOH656 4.9 35.1 1.0
CB A:GLU73 5.0 17.4 1.0

Copper binding site 3 out of 5 in 2aqq

Go back to Copper Binding Sites List in 2aqq
Copper binding site 3 out of 5 in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:16.6
occ:1.00
 NE2 B:HIS81 2.0 13.2 1.0
NE2 B:HIS160 2.1 13.8 1.0
ND1 B:HIS79 2.1 13.0 1.0
CE1 B:HIS81 2.9 14.6 1.0
CD2 B:HIS160 3.0 12.5 1.0
CE1 B:HIS79 3.0 13.4 1.0
CD2 B:HIS81 3.1 13.5 1.0
CE1 B:HIS160 3.1 14.8 1.0
CG B:HIS79 3.1 12.8 1.0
NE2 B:HIS104 3.2 16.7 1.0
CB B:HIS79 3.5 13.7 1.0
CD2 B:HIS104 3.5 16.8 1.0
O B:HOH527 3.7 23.8 1.0
CB B:MET158 3.8 13.6 1.0
CE1 B:HIS104 4.0 17.7 1.0
CG B:MET158 4.0 13.7 1.0
ND1 B:HIS81 4.1 13.1 1.0
NE2 B:HIS79 4.1 11.3 1.0
CG B:HIS160 4.1 12.8 1.0
ND1 B:HIS160 4.2 13.3 1.0
CG B:HIS81 4.2 13.2 1.0
O B:HOH529 4.2 17.5 1.0
CD2 B:HIS79 4.2 12.5 1.0
N B:HIS79 4.3 12.8 1.0
CA B:HIS79 4.3 13.7 1.0
CG B:HIS104 4.5 16.1 1.0
O B:HIS79 4.5 14.2 1.0
C B:HIS79 4.6 14.7 1.0
O B:MET158 4.7 14.7 1.0
ND1 B:HIS104 4.7 15.4 1.0
CA B:MET158 5.0 14.0 1.0
C B:MET158 5.0 14.0 1.0

Copper binding site 4 out of 5 in 2aqq

Go back to Copper Binding Sites List in 2aqq
Copper binding site 4 out of 5 in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu200

b:15.5
occ:1.00
 NE2 C:HIS81 2.0 11.7 1.0
NE2 C:HIS160 2.0 11.9 1.0
ND1 C:HIS79 2.1 11.4 1.0
CD2 C:HIS160 2.9 12.4 1.0
CE1 C:HIS81 3.0 14.9 1.0
CD2 C:HIS81 3.0 13.7 1.0
CE1 C:HIS79 3.0 11.8 1.0
CG C:HIS79 3.1 11.7 1.0
CE1 C:HIS160 3.1 12.6 1.0
NE2 C:HIS104 3.2 15.1 1.0
CB C:HIS79 3.4 11.8 1.0
CD2 C:HIS104 3.5 14.9 1.0
O C:HOH705 3.5 23.3 1.0
CB C:MET158 3.8 13.5 1.0
CG C:MET158 4.0 14.2 1.0
CE1 C:HIS104 4.0 16.2 1.0
ND1 C:HIS81 4.1 12.2 1.0
CG C:HIS160 4.1 10.8 1.0
O C:HOH629 4.1 22.9 1.0
NE2 C:HIS79 4.1 11.3 1.0
ND1 C:HIS160 4.2 12.5 1.0
CG C:HIS81 4.2 10.3 1.0
CD2 C:HIS79 4.2 11.0 1.0
N C:HIS79 4.3 11.0 1.0
CA C:HIS79 4.3 10.9 1.0
CG C:HIS104 4.5 13.8 1.0
O C:HIS79 4.6 10.3 1.0
O C:MET158 4.7 12.4 1.0
C C:HIS79 4.7 11.0 1.0
ND1 C:HIS104 4.7 14.1 1.0
C C:MET158 5.0 12.6 1.0

Copper binding site 5 out of 5 in 2aqq

Go back to Copper Binding Sites List in 2aqq
Copper binding site 5 out of 5 in the Cu/Zn Superoxid Dismutate From Neisseria Meningitidis K91E 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu251

b:7.0
occ:0.50
 ND1 C:HIS133 1.9 19.3 1.0
OE1 C:GLU73 2.1 19.9 1.0
CE1 C:HIS133 2.8 18.4 1.0
CD C:GLU73 2.8 24.2 1.0
OE2 C:GLU73 2.8 25.5 1.0
CG C:HIS133 3.0 17.2 1.0
CB C:HIS133 3.4 16.8 1.0
NE2 C:HIS133 3.9 17.3 1.0
CD2 C:HIS133 4.0 17.8 1.0
CA C:HIS133 4.0 19.1 1.0
CG C:GLU73 4.3 23.5 1.0
O C:HOH506 4.3 21.3 1.0
N C:HIS133 4.8 16.7 1.0
CB C:GLU73 4.9 22.0 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 Superoxid Dismutate From Neisseria Meningitidis K91E Mutant To Be Published.
Page generated: Tue Jul 30 23:11:52 2024

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