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Copper in PDB 1pzs: Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution

Enzymatic activity of Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution

All present enzymatic activity of Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution, PDB code: 1pzs was solved by K.Djinovic-Carugo, L.Spagnolo, I.Toro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.95 / 1.63
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.040, 58.420, 51.390, 90.00, 126.99, 90.00
R / Rfree (%) 15 / 19

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution (pdb code 1pzs). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution, PDB code: 1pzs:

Copper binding site 1 out of 1 in 1pzs

Go back to Copper Binding Sites List in 1pzs
Copper binding site 1 out of 1 in the Crystal Structure of A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution


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 A Cu-Zn Superoxide Dismutase From Mycobacterium Tuberculosis at 1.63 Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu172

b:20.8
occ:0.75
 O A:HOH448 1.9 25.6 1.0
NE2 A:HIS126 2.0 15.3 1.0
NE2 A:HIS49 2.0 15.5 1.0
ND1 A:HIS47 2.1 16.3 1.0
CG A:HIS47 2.9 12.5 1.0
CE1 A:HIS49 2.9 12.9 1.0
CD2 A:HIS126 3.0 15.0 1.0
CE1 A:HIS126 3.1 13.2 1.0
CD2 A:HIS49 3.1 12.8 1.0
CB A:HIS47 3.1 12.2 1.0
CE1 A:HIS47 3.1 18.3 1.0
NE2 A:HIS75 3.3 22.4 1.0
CD2 A:HIS75 3.7 21.5 1.0
O A:HOH452 3.7 37.8 1.0
O A:HOH449 3.8 36.3 1.0
ND1 A:HIS49 4.1 11.7 1.0
CD2 A:HIS47 4.1 14.4 1.0
CA A:HIS47 4.1 10.3 1.0
CG A:HIS126 4.1 10.0 1.0
N A:HIS47 4.1 9.4 1.0
ND1 A:HIS126 4.2 12.4 1.0
CG A:HIS49 4.2 10.8 1.0
NE2 A:HIS47 4.2 15.3 1.0
CE1 A:HIS75 4.3 23.0 1.0
O A:HIS47 4.4 9.3 1.0
CB A:ILE124 4.5 10.0 1.0
C A:HIS47 4.5 10.2 1.0
CG2 A:ILE124 4.6 12.4 1.0
O A:ILE124 4.8 8.9 1.0
CG A:HIS75 4.8 19.9 1.0

Reference:

L.Spagnolo, I.Toro, M.D'orazio, P.O'neill, J.Z.Pedersen, O.Carugo, G.Rotilio, A.Battistoni, K.Djinovic-Carugo. Unique Features of the Sodc-Encoded Superoxide Dismutase From Mycobacterium Tuberculosis, A Fully Functional Copper-Containing Enzyme Lacking Zinc in the Active Site. J.Biol.Chem. V. 279 33447 2004.
ISSN: ISSN 0021-9258
PubMed: 15155722
DOI: 10.1074/JBC.M404699200
Page generated: Mon Jul 14 00:17:50 2025

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