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Copper in PDB 2j55: X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin.

Enzymatic activity of X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin.

All present enzymatic activity of X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin.:
1.4.99.3;

Protein crystallography data

The structure of X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin., PDB code: 2j55 was solved by A.R.Pearson, R.Pahl, V.L.Davidson, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 21.70 / 2.15
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 122.733, 122.733, 246.591, 90.00, 90.00, 90.00
R / Rfree (%) 18.9 / 24.5

Copper Binding Sites:

The binding sites of Copper atom in the X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin. (pdb code 2j55). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin., PDB code: 2j55:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2j55

Go back to Copper Binding Sites List in 2j55
Copper binding site 1 out of 2 in the X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1106

b:66.5
occ:1.00
SG A:CYS92 2.1 64.0 1.0
ND1 A:HIS95 2.3 52.7 1.0
ND1 A:HIS53 2.4 71.0 1.0
SD A:MET98 2.5 61.3 1.0
CG A:HIS53 3.0 70.4 1.0
CB A:HIS53 3.1 67.1 1.0
CB A:CYS92 3.2 63.1 1.0
CG A:HIS95 3.2 62.0 1.0
CE A:MET98 3.3 62.0 1.0
CE1 A:HIS95 3.3 60.9 1.0
CE1 A:HIS53 3.4 72.9 1.0
CB A:HIS95 3.4 63.2 1.0
CA A:HIS53 3.5 67.6 1.0
O A:PRO52 3.8 68.8 1.0
CD2 A:HIS53 4.1 73.0 1.0
CG A:MET98 4.3 56.9 1.0
NE2 A:HIS53 4.3 70.2 1.0
CD2 A:HIS95 4.4 63.5 1.0
N A:HIS53 4.4 67.7 1.0
NE2 A:HIS95 4.4 65.2 1.0
CG A:PRO94 4.5 62.0 1.0
C A:PRO52 4.5 68.0 1.0
N A:HIS95 4.5 65.9 1.0
CA A:HIS95 4.6 64.2 1.0
N A:ASN54 4.6 65.9 1.0
C A:HIS53 4.6 67.4 1.0
CA A:CYS92 4.6 64.0 1.0
CE A:MET28 4.7 66.1 1.0
CB A:MET98 4.9 63.1 1.0
O A:HIS95 5.0 67.1 1.0

Copper binding site 2 out of 2 in 2j55

Go back to Copper Binding Sites List in 2j55
Copper binding site 2 out of 2 in the X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of X-Ray Reduced Paraccocus Denitrificans Methylamine Dehydrogenase O-Quinone in Complex with Amicyanin. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu1106

b:65.1
occ:1.00
ND1 B:HIS95 1.8 43.2 1.0
SG B:CYS92 2.1 56.0 1.0
ND1 B:HIS53 2.1 50.7 1.0
CE1 B:HIS95 2.4 50.9 1.0
SD B:MET98 3.0 61.0 1.0
CG B:HIS95 3.0 55.2 1.0
CB B:CYS92 3.0 55.1 1.0
CE1 B:HIS53 3.1 48.1 1.0
CG B:HIS53 3.1 53.3 1.0
CB B:HIS53 3.5 54.8 1.0
CE B:MET98 3.6 59.1 1.0
NE2 B:HIS95 3.6 51.3 1.0
CA B:HIS53 3.7 53.8 1.0
CB B:HIS95 3.7 57.9 1.0
O B:PRO52 3.9 54.2 1.0
CD2 B:HIS95 3.9 49.1 1.0
NE2 B:HIS53 4.2 54.9 1.0
CD2 B:HIS53 4.2 56.3 1.0
CG B:MET98 4.3 58.5 1.0
N B:ASN54 4.4 53.3 1.0
CA B:CYS92 4.5 55.3 1.0
CG B:PRO94 4.5 55.5 1.0
C B:HIS53 4.6 52.6 1.0
N B:HIS53 4.7 53.5 1.0
C B:PRO52 4.7 54.5 1.0
N B:HIS95 4.7 56.7 1.0
CB B:MET98 4.7 59.6 1.0
CA B:HIS95 4.8 57.2 1.0
CD B:PRO94 5.0 56.2 1.0
C B:CYS92 5.0 56.0 1.0
CE B:MET28 5.0 62.2 1.0

Reference:

A.R.Pearson, R.Pahl, E.G.Kovaleva, V.L.Davidson, C.M.Wilmot. Tracking X-Ray-Derived Redox Changes in Crystals of A Methylamine Dehydrogenase/Amicyanin Complex Using Single-Crystal Uv/Vis Microspectrophotometry. J.Synchrotron Radiat. V. 14 92 2007.
ISSN: ISSN 0909-0495
PubMed: 17211075
DOI: 10.1107/S0909049506051259
Page generated: Wed Oct 28 14:20:11 2020
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