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

Copper in PDB 1dsw: The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein

Enzymatic activity of The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein

All present enzymatic activity of The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein:
1.15.1.1;

Other elements in 1dsw:

The structure of The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein (pdb code 1dsw). 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 The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein, PDB code: 1dsw:

Copper binding site 1 out of 1 in 1dsw

Go back to Copper Binding Sites List in 1dsw
Copper binding site 1 out of 1 in the The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The Solution Structure of A Monomeric, Reduced Form of Human Copper, Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:0.0
occ:1.00
 NE2 A:HIS48 2.0 0.0 1.0
ND1 A:HIS46 2.1 0.0 1.0
NE2 A:HIS120 2.2 0.0 1.0
CD2 A:HIS120 2.9 0.0 1.0
CG A:HIS46 3.0 0.0 1.0
CE1 A:HIS48 3.0 0.0 1.0
HD2 A:HIS120 3.0 0.0 1.0
HB2 A:HIS46 3.0 0.0 1.0
CD2 A:HIS48 3.0 0.0 1.0
HE2 A:HIS63 3.1 0.0 1.0
HE1 A:HIS48 3.2 0.0 1.0
HB A:VAL118 3.2 0.0 1.0
CE1 A:HIS46 3.3 0.0 1.0
H A:HIS46 3.3 0.0 1.0
HD2 A:HIS48 3.3 0.0 1.0
CE1 A:HIS120 3.3 0.0 1.0
CB A:HIS46 3.4 0.0 1.0
NE2 A:HIS63 3.5 0.0 1.0
O A:VAL118 3.6 0.0 1.0
HE1 A:HIS46 3.6 0.0 1.0
HE1 A:HIS120 3.7 0.0 1.0
N A:HIS46 3.7 0.0 1.0
O A:HIS46 3.8 0.0 1.0
CA A:HIS46 3.9 0.0 1.0
CD2 A:HIS63 4.0 0.0 1.0
C A:HIS46 4.0 0.0 1.0
H A:VAL118 4.1 0.0 1.0
CE1 A:HIS63 4.1 0.0 1.0
CG A:HIS120 4.1 0.0 1.0
ND1 A:HIS48 4.1 0.0 1.0
CG A:HIS48 4.1 0.0 1.0
HD2 A:HIS63 4.2 0.0 1.0
CD2 A:HIS46 4.2 0.0 1.0
CB A:VAL118 4.3 0.0 1.0
HE1 A:HIS63 4.3 0.0 1.0
NE2 A:HIS46 4.3 0.0 1.0
ND1 A:HIS120 4.3 0.0 1.0
HA A:PHE45 4.3 0.0 1.0
HB3 A:HIS46 4.4 0.0 1.0
C A:VAL118 4.4 0.0 1.0
C A:PHE45 4.5 0.0 1.0
HG13 A:VAL118 4.6 0.0 1.0
CA A:VAL118 4.7 0.0 1.0
N A:VAL118 4.7 0.0 1.0
HB A:THR137 4.9 0.0 1.0
CA A:PHE45 4.9 0.0 1.0
CG A:HIS63 4.9 0.0 1.0
CG1 A:VAL118 4.9 0.0 1.0
HA A:HIS46 4.9 0.0 1.0
N A:VAL47 5.0 0.0 1.0
ND1 A:HIS63 5.0 0.0 1.0

Reference:

L.Banci, I.Bertini, R.Del Conte, R.Fadin, S.Mangani, M.S.Viezzoli. The Solution Structure of A Monomeric, Reduced Form of Human Copper,Zinc Superoxide Dismutase Bearing the Same Charge As the Native Protein. J.Biol.Inorg.Chem. V. 4 795 1999.
ISSN: ISSN 0949-8257
PubMed: 10631612
DOI: 10.1007/S007750050353
Page generated: Tue Jul 30 21:42:46 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy