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Copper 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:

Zinc (Zn) 3 atoms

Copper Binding Sites:

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

Copper binding site 1 out of 5 in 2aqn

Go back to Copper Binding Sites List in 2aqn
Copper binding site 1 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:18.2
occ:1.00
 NE2 A:HIS81 1.9 16.1 1.0
ND1 A:HIS79 2.0 16.0 1.0
NE2 A:HIS160 2.1 15.0 1.0
CE1 A:HIS81 2.9 16.5 1.0
CD2 A:HIS160 3.0 16.0 1.0
CG A:HIS79 3.0 16.0 1.0
CD2 A:HIS81 3.0 17.7 1.0
CE1 A:HIS79 3.0 17.0 1.0
CE1 A:HIS160 3.1 15.4 1.0
NE2 A:HIS104 3.1 18.4 1.0
CB A:HIS79 3.3 16.6 1.0
CD2 A:HIS104 3.5 20.9 1.0
O A:HOH550 3.7 24.7 1.0
CB A:MET158 3.8 16.3 1.0
CE1 A:HIS104 4.0 20.5 1.0
ND1 A:HIS81 4.0 15.9 1.0
CG A:MET158 4.0 16.5 1.0
NE2 A:HIS79 4.1 15.4 1.0
CG A:HIS81 4.1 16.1 1.0
CD2 A:HIS79 4.1 16.1 1.0
CG A:HIS160 4.2 15.7 1.0
ND1 A:HIS160 4.2 16.2 1.0
O A:HOH573 4.3 24.6 1.0
CA A:HIS79 4.3 15.0 1.0
N A:HIS79 4.4 15.7 1.0
CG A:HIS104 4.5 16.8 1.0
O A:HIS79 4.6 16.6 1.0
ND1 A:HIS104 4.7 16.3 1.0
C A:HIS79 4.8 14.7 1.0
O A:MET158 4.9 16.5 1.0

Copper binding site 2 out of 5 in 2aqn

Go back to Copper Binding Sites List in 2aqn
Copper binding site 2 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu300

b:24.4
occ:0.93
 OE1 A:GLU73 1.9 32.5 1.0
ND1 B:HIS133 2.0 27.1 1.0
ND1 A:HIS133 2.0 23.5 1.0
OE1 B:GLU73 2.0 29.3 1.0
CD A:GLU73 2.7 28.4 1.0
OE2 A:GLU73 2.8 29.0 1.0
CD B:GLU73 2.8 30.9 1.0
OE2 B:GLU73 2.8 42.3 1.0
CE1 A:HIS133 2.9 24.8 1.0
CE1 B:HIS133 2.9 30.3 1.0
CG B:HIS133 2.9 24.2 1.0
CG A:HIS133 3.1 18.5 1.0
CB B:HIS133 3.4 21.8 1.0
CB A:HIS133 3.5 16.9 1.0
CA B:HIS133 3.9 22.6 1.0
NE2 B:HIS133 4.0 30.6 1.0
CD2 B:HIS133 4.1 27.0 1.0
NE2 A:HIS133 4.1 26.9 1.0
CG A:GLU73 4.1 28.9 1.0
CD2 A:HIS133 4.1 22.9 1.0
CA A:HIS133 4.2 18.0 1.0
CG B:GLU73 4.2 29.9 1.0
O B:HOH726 4.3 25.5 1.0
O B:HOH732 4.4 30.1 1.0
N B:HIS133 4.7 22.3 1.0
O A:HOH618 4.7 39.9 1.0
CB B:GLU73 4.7 25.2 1.0
N A:HIS133 4.8 19.2 1.0

Copper binding site 3 out of 5 in 2aqn

Go back to Copper Binding Sites List in 2aqn
Copper binding site 3 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:19.2
occ:1.00
 NE2 B:HIS81 2.0 16.2 1.0
ND1 B:HIS79 2.0 16.1 1.0
NE2 B:HIS160 2.0 17.5 1.0
CE1 B:HIS81 2.9 18.3 1.0
CG B:HIS79 3.0 16.7 1.0
CE1 B:HIS79 3.0 16.8 1.0
CD2 B:HIS160 3.0 16.7 1.0
CD2 B:HIS81 3.0 17.6 1.0
CE1 B:HIS160 3.1 18.7 1.0
NE2 B:HIS104 3.2 21.6 1.0
CB B:HIS79 3.4 17.6 1.0
O B:HOH512 3.5 29.9 1.0
CD2 B:HIS104 3.5 21.9 1.0
CB B:MET158 3.8 17.3 1.0
CG B:MET158 4.0 18.3 1.0
CE1 B:HIS104 4.0 21.0 1.0
ND1 B:HIS81 4.1 17.7 1.0
CD2 B:HIS79 4.1 16.0 1.0
NE2 B:HIS79 4.1 16.8 1.0
CG B:HIS81 4.1 16.6 1.0
ND1 B:HIS160 4.1 18.6 1.0
CG B:HIS160 4.2 16.2 1.0
O B:HOH578 4.3 27.5 1.0
CA B:HIS79 4.3 17.5 1.0
N B:HIS79 4.3 17.5 1.0
CG B:HIS104 4.5 19.2 1.0
O B:HIS79 4.6 18.9 1.0
O B:MET158 4.7 18.5 1.0
ND1 B:HIS104 4.7 18.8 1.0
C B:HIS79 4.7 18.5 1.0
CA B:MET158 5.0 16.7 1.0

Copper binding site 4 out of 5 in 2aqn

Go back to Copper Binding Sites List in 2aqn
Copper binding site 4 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu200

b:17.4
occ:1.00
 NE2 C:HIS160 1.9 15.8 1.0
NE2 C:HIS81 2.0 16.3 1.0
ND1 C:HIS79 2.0 15.4 1.0
CD2 C:HIS160 2.9 15.7 1.0
CE1 C:HIS160 3.0 17.6 1.0
CE1 C:HIS81 3.0 17.6 1.0
CD2 C:HIS81 3.0 17.1 1.0
CE1 C:HIS79 3.0 17.7 1.0
CG C:HIS79 3.0 15.2 1.0
NE2 C:HIS104 3.1 17.9 1.0
CB C:HIS79 3.4 15.7 1.0
O C:HOH658 3.5 28.8 1.0
CD2 C:HIS104 3.5 19.8 1.0
CB C:MET158 3.8 16.4 1.0
CG C:MET158 3.9 18.5 1.0
CE1 C:HIS104 4.0 17.2 1.0
ND1 C:HIS160 4.1 16.9 1.0
ND1 C:HIS81 4.1 16.8 1.0
CG C:HIS160 4.1 15.4 1.0
CG C:HIS81 4.1 14.7 1.0
NE2 C:HIS79 4.1 16.1 1.0
CD2 C:HIS79 4.2 14.1 1.0
O C:HOH517 4.3 28.1 1.0
CA C:HIS79 4.4 15.1 1.0
N C:HIS79 4.4 14.4 1.0
CG C:HIS104 4.6 16.3 1.0
O C:HIS79 4.6 15.4 1.0
O C:MET158 4.7 16.9 1.0
C C:HIS79 4.7 15.8 1.0
ND1 C:HIS104 4.8 15.8 1.0

Copper binding site 5 out of 5 in 2aqn

Go back to Copper Binding Sites List in 2aqn
Copper binding site 5 out of 5 in the Cu/Zn Superoxide Dismutase From Neisseria Meningitidis


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu301

b:29.1
occ:0.54
 ND1 C:HIS133 2.1 27.1 1.0
OE1 C:GLU73 2.1 33.6 1.0
OE2 C:GLU73 2.7 60.2 1.0
CD C:GLU73 2.8 39.0 1.0
CE1 C:HIS133 3.0 26.6 1.0
CG C:HIS133 3.1 23.3 1.0
CB C:HIS133 3.4 21.7 1.0
CA C:HIS133 4.1 20.6 1.0
NE2 C:HIS133 4.1 27.1 1.0
CD2 C:HIS133 4.2 26.2 1.0
CG C:GLU73 4.3 29.7 1.0
O C:HOH702 4.6 37.5 1.0
O C:HOH765 4.7 36.1 1.0
N C:HIS133 4.8 22.2 1.0
CB C:GLU73 4.9 24.3 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 To Be Published.
Page generated: Tue Jul 30 23:11:52 2024

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