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Copper in PDB 1ptz: Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R

Enzymatic activity of Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R

All present enzymatic activity of Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R, PDB code: 1ptz was solved by M.Didonato, L.Craig, M.E.Huff, M.M.Thayer, R.M.F.Cardoso, C.J.Kassmann, T.P.Lo, C.K.Bruns, E.T.Powers, J.W.Kelly, E.D.Getzoff, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.05 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 111.199, 47.525, 56.041, 90.00, 97.99, 90.00
R / Rfree (%) 18.6 / 21.5

Other elements in 1ptz:

The structure of Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R (pdb code 1ptz). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R, PDB code: 1ptz:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ptz

Go back to Copper Binding Sites List in 1ptz
Copper binding site 1 out of 2 in the Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R


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 the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu200

b:22.9
occ:1.00
NE2 A:HIS48 2.0 16.7 1.0
NE2 A:HIS120 2.0 15.2 1.0
ND1 A:HIS46 2.1 18.4 1.0
CE1 A:HIS48 3.0 15.7 1.0
CD2 A:HIS120 3.0 16.6 1.0
CD2 A:HIS48 3.0 17.3 1.0
CE1 A:HIS120 3.1 16.8 1.0
CG A:HIS46 3.1 19.4 1.0
NE2 A:HIS63 3.2 22.4 1.0
CE1 A:HIS46 3.2 17.3 1.0
CB A:HIS46 3.3 18.0 1.0
CD2 A:HIS63 3.5 21.6 1.0
O A:HOH350 3.6 25.0 1.0
ND1 A:HIS48 4.1 15.0 1.0
CB A:VAL118 4.1 18.5 1.0
CE1 A:HIS63 4.1 21.2 1.0
CG A:HIS48 4.1 15.4 1.0
ND1 A:HIS120 4.1 16.1 1.0
CG A:HIS120 4.1 16.2 1.0
N A:HIS46 4.2 16.0 1.0
CA A:HIS46 4.2 17.2 1.0
CD2 A:HIS46 4.2 18.0 1.0
NE2 A:HIS46 4.2 19.6 1.0
CG1 A:VAL118 4.3 17.3 1.0
O A:HIS46 4.6 15.5 1.0
C A:HIS46 4.6 16.7 1.0
CG A:HIS63 4.6 20.0 1.0
O A:VAL118 4.6 16.7 1.0
CG2 A:VAL118 4.9 15.9 1.0
ND1 A:HIS63 4.9 19.5 1.0

Copper binding site 2 out of 2 in 1ptz

Go back to Copper Binding Sites List in 1ptz
Copper binding site 2 out of 2 in the Crystal Structure of the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R


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 the Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43R within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu200

b:26.8
occ:1.00
NE2 B:HIS48 1.9 20.1 1.0
NE2 B:HIS120 2.1 21.0 1.0
ND1 B:HIS46 2.2 22.2 1.0
CE1 B:HIS48 2.9 21.1 1.0
CD2 B:HIS48 2.9 20.2 1.0
CD2 B:HIS120 3.0 21.1 1.0
NE2 B:HIS63 3.0 21.7 1.0
CE1 B:HIS120 3.0 21.6 1.0
CE1 B:HIS46 3.1 20.6 1.0
CG B:HIS46 3.2 20.1 1.0
O B:HOH417 3.3 32.6 1.0
CD2 B:HIS63 3.4 22.3 1.0
CB B:HIS46 3.5 21.7 1.0
ND1 B:HIS48 4.0 19.8 1.0
CE1 B:HIS63 4.0 21.1 1.0
CG B:HIS48 4.1 18.6 1.0
ND1 B:HIS120 4.2 20.7 1.0
CG B:HIS120 4.2 21.4 1.0
CB B:VAL118 4.2 20.3 1.0
NE2 B:HIS46 4.2 20.9 1.0
CD2 B:HIS46 4.3 20.1 1.0
N B:HIS46 4.3 18.1 1.0
CA B:HIS46 4.4 18.0 1.0
CG1 B:VAL118 4.4 20.4 1.0
CG B:HIS63 4.5 21.1 1.0
O B:HIS46 4.6 15.2 1.0
C B:HIS46 4.7 18.3 1.0
ND1 B:HIS63 4.8 19.3 1.0
O B:VAL118 4.8 17.4 1.0
CG2 B:VAL118 4.9 19.8 1.0

Reference:

M.Didonato, L.Craig, M.E.Huff, M.M.Thayer, R.M.F.Cardoso, C.J.Kassmann, T.P.Lo, C.K.Bruns, E.T.Powers, J.W.Kelly, E.D.Getzoff, J.A.Tainer. Als Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization J.Mol.Biol. V. 332 601 2003.
ISSN: ISSN 0022-2836
PubMed: 12963370
DOI: 10.1016/S0022-2836(03)00889-1
Page generated: Wed Oct 28 14:16:43 2020
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