Atomistry » Copper » PDB 1bex-1eqw » 1eqw
Atomistry »
  Copper »
    PDB 1bex-1eqw »
      1eqw »

Copper in PDB 1eqw: Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase

Enzymatic activity of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase

All present enzymatic activity of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase, PDB code: 1eqw was solved by A.Pesce, A.Battistoni, M.E.Stroppolo, F.Polizio, M.Nardini, J.S.Kroll, P.R.Langford, P.O'neill, M.Sette, A.Desideri, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.60 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.140, 40.659, 114.254, 90.00, 107.73, 90.00
R / Rfree (%) 22.6 / 28.3

Other elements in 1eqw:

The structure of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 4 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase (pdb code 1eqw). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase, PDB code: 1eqw:
Jump to Copper binding site number: 1; 2; 3; 4;

Copper binding site 1 out of 4 in 1eqw

Go back to Copper Binding Sites List in 1eqw
Copper binding site 1 out of 4 in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:42.9
occ:1.00
 NE2 A:HIS118 1.9 37.9 1.0
NE2 A:HIS46 2.0 33.6 1.0
ND1 A:HIS44 2.3 38.1 1.0
NE2 A:HIS61 2.5 48.6 1.0
CE1 A:HIS118 2.8 35.9 1.0
CE1 A:HIS46 2.9 28.9 1.0
CD2 A:HIS118 3.0 33.3 1.0
CD2 A:HIS61 3.1 50.4 1.0
CD2 A:HIS46 3.1 37.1 1.0
CE1 A:HIS44 3.2 36.7 1.0
CG A:HIS44 3.3 35.4 1.0
CE1 A:HIS61 3.4 48.1 1.0
CB A:HIS44 3.6 36.2 1.0
ND1 A:HIS118 4.0 32.4 1.0
CB A:MET116 4.0 36.0 1.0
ND1 A:HIS46 4.1 35.0 1.0
CG A:HIS118 4.1 34.1 1.0
CG A:HIS61 4.1 39.0 1.0
CG A:MET116 4.2 39.4 1.0
CG A:HIS46 4.2 37.4 1.0
ND1 A:HIS61 4.3 41.5 1.0
NE2 A:HIS44 4.4 36.2 1.0
CD2 A:HIS44 4.4 38.9 1.0
N A:HIS44 4.5 41.1 1.0
CA A:HIS44 4.5 37.3 1.0
O A:HIS44 4.8 34.1 1.0
C A:HIS44 4.8 36.1 1.0

Copper binding site 2 out of 4 in 1eqw

Go back to Copper Binding Sites List in 1eqw
Copper binding site 2 out of 4 in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu504

b:50.4
occ:1.00
 NE2 B:HIS118 2.0 40.6 1.0
NE2 B:HIS46 2.2 34.8 1.0
ND1 B:HIS44 2.2 42.5 1.0
NE2 B:HIS61 2.5 48.4 1.0
CE1 B:HIS118 2.8 34.2 1.0
CE1 B:HIS46 3.0 33.9 1.0
CD2 B:HIS118 3.0 34.5 1.0
CE1 B:HIS44 3.1 40.4 1.0
CD2 B:HIS61 3.1 44.6 1.0
CG B:HIS44 3.2 43.4 1.0
CD2 B:HIS46 3.3 36.3 1.0
CE1 B:HIS61 3.5 46.6 1.0
CB B:HIS44 3.6 40.6 1.0
ND1 B:HIS118 4.0 36.7 1.0
CG B:HIS118 4.1 36.2 1.0
ND1 B:HIS46 4.2 36.8 1.0
CB B:MET116 4.2 31.6 1.0
NE2 B:HIS44 4.2 39.2 1.0
CG B:HIS61 4.3 46.5 1.0
CD2 B:HIS44 4.3 39.8 1.0
CG B:HIS46 4.3 40.6 1.0
CG B:MET116 4.3 34.1 1.0
ND1 B:HIS61 4.4 44.7 1.0
N B:HIS44 4.6 37.4 1.0
CA B:HIS44 4.6 37.0 1.0
O B:HIS44 4.9 40.2 1.0
C B:HIS44 5.0 38.0 1.0

Copper binding site 3 out of 4 in 1eqw

Go back to Copper Binding Sites List in 1eqw
Copper binding site 3 out of 4 in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu506

b:38.1
occ:1.00
 NE2 C:HIS118 1.9 35.7 1.0
NE2 C:HIS46 2.1 35.8 1.0
ND1 C:HIS44 2.2 33.5 1.0
NE2 C:HIS61 2.7 42.7 1.0
CE1 C:HIS118 2.8 34.0 1.0
CE1 C:HIS46 3.0 34.9 1.0
CD2 C:HIS118 3.0 36.8 1.0
CE1 C:HIS44 3.1 33.1 1.0
CD2 C:HIS46 3.2 38.5 1.0
O C:HOH543 3.2 39.2 1.0
CG C:HIS44 3.2 34.5 1.0
CD2 C:HIS61 3.2 42.0 1.0
CB C:HIS44 3.5 31.9 1.0
CE1 C:HIS61 3.8 44.5 1.0
ND1 C:HIS118 4.0 38.8 1.0
CG C:MET116 4.0 21.4 1.0
CB C:MET116 4.1 27.3 1.0
CG C:HIS118 4.1 35.8 1.0
ND1 C:HIS46 4.1 40.9 1.0
CG C:HIS46 4.3 36.2 1.0
NE2 C:HIS44 4.3 35.6 1.0
CD2 C:HIS44 4.3 34.6 1.0
N C:HIS44 4.4 33.6 1.0
CG C:HIS61 4.4 40.3 1.0
CA C:HIS44 4.5 31.3 1.0
ND1 C:HIS61 4.7 32.6 1.0
O C:HIS44 4.8 33.3 1.0
C C:HIS44 4.8 32.7 1.0

Copper binding site 4 out of 4 in 1eqw

Go back to Copper Binding Sites List in 1eqw
Copper binding site 4 out of 4 in the Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Salmonella Typhimurium Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Cu508

b:47.8
occ:1.00
 NE2 D:HIS118 1.9 39.8 1.0
ND1 D:HIS44 2.0 39.0 1.0
NE2 D:HIS46 2.2 40.6 1.0
CE1 D:HIS118 2.9 35.8 1.0
CD2 D:HIS118 2.9 37.6 1.0
CE1 D:HIS44 3.0 39.1 1.0
CG D:HIS44 3.0 45.6 1.0
CE1 D:HIS46 3.1 35.9 1.0
NE2 D:HIS61 3.2 59.6 1.0
CD2 D:HIS46 3.2 40.9 1.0
CB D:HIS44 3.4 43.6 1.0
CD2 D:HIS61 3.7 56.2 1.0
CE1 D:HIS61 3.8 58.8 1.0
ND1 D:HIS118 4.0 31.8 1.0
CB D:MET116 4.1 36.3 1.0
CG D:HIS118 4.1 35.3 1.0
NE2 D:HIS44 4.1 40.5 1.0
CD2 D:HIS44 4.2 43.4 1.0
CG D:MET116 4.3 28.8 1.0
ND1 D:HIS46 4.3 33.4 1.0
N D:HIS44 4.3 38.9 1.0
CG D:HIS46 4.3 37.8 1.0
CA D:HIS44 4.4 39.7 1.0
CG D:HIS61 4.5 59.3 1.0
ND1 D:HIS61 4.5 56.2 1.0
O D:HIS44 4.7 41.7 1.0
C D:HIS44 4.7 41.2 1.0
O D:MET116 5.0 34.9 1.0

Reference:

A.Pesce, A.Battistoni, M.E.Stroppolo, F.Polizio, M.Nardini, J.S.Kroll, P.R.Langford, P.O'neill, M.Sette, A.Desideri, M.Bolognesi. Functional and Crystallographic Characterization of Salmonella Typhimurium Cu,Zn Superoxide Dismutase Coded By the Sodci Virulence Gene. J.Mol.Biol. V. 302 465 2000.
ISSN: ISSN 0022-2836
PubMed: 10970746
DOI: 10.1006/JMBI.2000.4074
Page generated: Tue Jul 30 21:44:55 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy