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Copper in PDB 1mfm: Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution

Enzymatic activity of Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution

All present enzymatic activity of Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution:
1.15.1.1;

Protein crystallography data

The structure of Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution, PDB code: 1mfm was solved by M.Ferraroni, W.Rypniewski, K.S.Wilson, P.L.Orioli, M.S.Viezzoli, L.Banci, I.Bertini, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 34.990, 48.110, 81.080, 90.00, 90.00, 90.00
R / Rfree (%) 11.8 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution (pdb code 1mfm). 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 Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution, PDB code: 1mfm:

Copper binding site 1 out of 1 in 1mfm

Go back to Copper Binding Sites List in 1mfm
Copper binding site 1 out of 1 in the Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu155

b:10.0
occ:0.41
CD A:CD164 1.6 90.8 0.5
ND1 A:HIS46 2.0 12.3 1.0
NE2 A:HIS48 2.0 13.2 1.0
NE2 A:HIS120 2.2 13.4 1.0
CG A:HIS46 2.8 11.2 1.0
CB A:HIS46 2.9 15.2 1.0
CD2 A:HIS120 2.9 11.7 1.0
CD2 A:HIS48 2.9 14.7 1.0
CE1 A:HIS48 3.1 17.5 1.0
CE1 A:HIS46 3.1 11.6 1.0
NE2 A:HIS63 3.3 11.7 1.0
CE1 A:HIS120 3.4 13.8 1.0
O A:HOH176 3.7 13.0 1.0
CD2 A:HIS63 3.8 11.6 1.0
O A:HOH224 4.0 23.1 1.0
CD2 A:HIS46 4.0 12.4 1.0
CA A:HIS46 4.0 9.4 1.0
N A:HIS46 4.1 8.9 1.0
CB A:VAL118 4.1 9.9 1.0
CG1 A:VAL118 4.1 12.0 1.0
NE2 A:HIS46 4.1 10.4 1.0
CG A:HIS48 4.1 10.0 1.0
CG A:HIS120 4.2 10.7 1.0
CE1 A:HIS63 4.2 10.5 1.0
ND1 A:HIS48 4.2 18.1 1.0
ND1 A:HIS120 4.3 13.0 1.0
C A:HIS46 4.5 9.0 1.0
O A:HIS46 4.5 9.0 1.0
O A:VAL118 4.5 10.0 1.0
CG A:HIS63 4.8 10.5 1.0
CG2 A:VAL118 4.9 12.6 1.0
O A:HOH300 4.9 34.0 1.0
C A:PHE45 4.9 9.2 1.0
ND1 A:HIS63 5.0 9.8 1.0

Reference:

M.Ferraroni, W.Rypniewski, K.S.Wilson, M.S.Viezzoli, L.Banci, I.Bertini, S.Mangani. The Crystal Structure of the Monomeric Human Sod Mutant F50E/G51E/E133Q at Atomic Resolution. the Enzyme Mechanism Revisited. J.Mol.Biol. V. 288 413 1999.
ISSN: ISSN 0022-2836
PubMed: 10329151
DOI: 10.1006/JMBI.1999.2681
Page generated: Thu Sep 3 16:08:08 2020
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