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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: Sun Dec 13 10:58:24 2020

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