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Copper in PDB 1spd: Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

Enzymatic activity of Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase

All present enzymatic activity of Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase, PDB code: 1spd was solved by H.E.Parge, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 5.00 / 2.40
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 113.570, 113.570, 71.550, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Other elements in 1spd:

The structure of Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase (pdb code 1spd). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase, PDB code: 1spd:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1spd

Go back to Copper Binding Sites List in 1spd
Copper binding site 1 out of 2 in the Amyotrophic Lateral Sclerosis and Structural Defects in 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 Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:6.3
occ:1.00
ND1 A:HIS46 2.0 9.9 1.0
NE2 A:HIS120 2.1 2.0 1.0
NE2 A:HIS63 2.1 8.9 1.0
NE2 A:HIS48 2.1 11.9 1.0
CE1 A:HIS120 2.7 2.0 1.0
CG A:HIS46 2.7 9.2 1.0
CB A:HIS46 2.9 6.7 1.0
CE1 A:HIS48 2.9 12.7 1.0
CE1 A:HIS63 3.0 8.6 1.0
CE1 A:HIS46 3.0 11.9 1.0
CD2 A:HIS63 3.0 6.7 1.0
CD2 A:HIS120 3.1 2.0 1.0
CD2 A:HIS48 3.2 13.2 1.0
ND1 A:HIS120 3.7 2.0 1.0
CD2 A:HIS46 3.7 9.8 1.0
NE2 A:HIS46 3.9 12.5 1.0
CG A:HIS120 4.0 2.0 1.0
ND1 A:HIS63 4.0 8.0 1.0
CG A:HIS63 4.1 6.3 1.0
ND1 A:HIS48 4.1 12.2 1.0
CG A:HIS48 4.3 12.9 1.0
CA A:HIS46 4.5 7.1 1.0
N A:HIS46 4.9 6.0 1.0
CG1 A:VAL118 4.9 11.4 1.0
O A:VAL47 4.9 4.2 1.0

Copper binding site 2 out of 2 in 1spd

Go back to Copper Binding Sites List in 1spd
Copper binding site 2 out of 2 in the Amyotrophic Lateral Sclerosis and Structural Defects in 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 Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu154

b:13.8
occ:1.00
NE2 B:HIS120 2.0 5.5 1.0
NE2 B:HIS48 2.1 10.4 1.0
NE2 B:HIS63 2.1 12.6 1.0
ND1 B:HIS46 2.2 19.0 1.0
CE1 B:HIS120 2.5 5.1 1.0
CE1 B:HIS48 2.9 9.4 1.0
CE1 B:HIS63 3.0 13.1 1.0
CG B:HIS46 3.0 18.6 1.0
CE1 B:HIS46 3.1 17.7 1.0
CD2 B:HIS120 3.1 4.2 1.0
CD2 B:HIS63 3.1 10.6 1.0
CB B:HIS46 3.3 18.9 1.0
CD2 B:HIS48 3.3 9.7 1.0
ND1 B:HIS120 3.5 2.0 1.0
CG B:HIS120 3.8 3.1 1.0
ND1 B:HIS48 4.1 6.0 1.0
NE2 B:HIS46 4.1 19.4 1.0
CD2 B:HIS46 4.1 18.9 1.0
ND1 B:HIS63 4.2 13.6 1.0
CG B:HIS63 4.2 13.4 1.0
CG B:HIS48 4.3 8.3 1.0
CG1 B:VAL118 4.5 4.7 1.0
CA B:HIS46 4.8 15.8 1.0
CG2 B:THR137 5.0 4.8 1.0

Reference:

H.X.Deng, A.Hentati, J.A.Tainer, Z.Iqbal, A.Cayabyab, W.Y.Hung, E.D.Getzoff, P.Hu, B.Herzfeldt, R.P.Roos, C.Warner, G.Deng, E.Soriano, C.Smyth, H.E.Parge, A.Ahmed, A.D.Roses, R.A.Hallewell, M.A.Pericak-Vance, T.Siddique. Amyotrophic Lateral Sclerosis and Structural Defects in Cu,Zn Superoxide Dismutase. Science V. 261 1047 1993.
ISSN: ISSN 0036-8075
PubMed: 8351519
Page generated: Sun Dec 13 11:02:02 2020

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