Atomistry » Copper » PDB 2aps-2cg1 » 2aqn
Atomistry »
  Copper »
    PDB 2aps-2cg1 »
      2aqn »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy