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Copper in PDB 1mda: Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin

Enzymatic activity of Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin

All present enzymatic activity of Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin, PDB code: 1mda was solved by L.Chen, R.Durley, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 124.700, 124.700, 247.400, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin (pdb code 1mda). 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 An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin, PDB code: 1mda:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1mda

Go back to Copper Binding Sites List in 1mda
Copper binding site 1 out of 2 in the Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin


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 An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu0

b:10.0
occ:1.00
ND1 A:HIS53 2.1 35.3 1.0
SG A:CYS92 2.1 15.6 1.0
ND1 A:HIS95 2.1 36.5 1.0
CE1 A:HIS95 2.5 20.5 1.0
CE1 A:HIS53 2.6 30.7 1.0
CB A:CYS92 2.8 35.7 1.0
SD A:MET98 2.9 46.2 1.0
CE A:MET98 3.0 47.4 1.0
CG A:HIS53 3.2 29.7 1.0
CG A:HIS95 3.5 50.0 1.0
NE2 A:HIS53 3.7 22.6 1.0
NE2 A:HIS95 3.7 11.6 1.0
CB A:HIS53 3.9 50.0 1.0
CD2 A:HIS53 4.0 10.0 1.0
CG A:MET98 4.1 27.6 1.0
CB A:HIS95 4.2 39.6 1.0
CD2 A:HIS95 4.2 10.0 1.0
CA A:CYS92 4.3 17.0 1.0
O A:HIS95 4.5 37.0 1.0
CA A:HIS53 4.6 50.0 1.0
O A:PRO52 4.6 12.3 1.0
C A:CYS92 4.7 26.2 1.0
O A:CYS92 4.8 40.5 1.0
CG A:PRO94 4.8 50.0 1.0
CD A:PRO94 5.0 40.5 1.0
N A:HIS95 5.0 17.6 1.0

Copper binding site 2 out of 2 in 1mda

Go back to Copper Binding Sites List in 1mda
Copper binding site 2 out of 2 in the Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin


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 An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu0

b:10.0
occ:1.00
ND1 B:HIS53 2.1 36.3 1.0
SG B:CYS92 2.1 30.2 1.0
ND1 B:HIS95 2.1 50.0 1.0
CE1 B:HIS95 2.2 39.8 1.0
CE B:MET98 2.2 34.1 1.0
CE1 B:HIS53 2.7 18.3 1.0
SD B:MET98 2.9 38.3 1.0
CB B:CYS92 2.9 10.0 1.0
CG B:HIS53 3.3 45.8 1.0
NE2 B:HIS95 3.5 50.0 1.0
CG B:HIS95 3.5 20.7 1.0
CG B:MET98 3.5 10.0 1.0
NE2 B:HIS53 3.9 38.6 1.0
CB B:HIS53 3.9 24.0 1.0
CD2 B:HIS95 4.1 10.0 1.0
CE B:MET28 4.2 50.0 1.0
CD2 B:HIS53 4.2 50.0 1.0
CB B:HIS95 4.4 10.0 1.0
CA B:CYS92 4.4 50.0 1.0
CB B:MET98 4.6 21.2 1.0
CA B:HIS53 4.7 50.0 1.0
O B:PRO52 4.7 10.0 1.0
O B:HIS95 4.7 28.8 1.0
O B:CYS92 4.9 37.9 1.0
C B:CYS92 4.9 32.5 1.0

Reference:

L.Chen, R.Durley, B.J.Poliks, K.Hamada, Z.Chen, F.S.Mathews, V.L.Davidson, Y.Satow, E.Huizinga, F.M.Vellieux, W.G.J.Hol. Crystal Structure of An Electron-Transfer Complex Between Methylamine Dehydrogenase and Amicyanin. Biochemistry V. 31 4959 1992.
ISSN: ISSN 0006-2960
PubMed: 1599920
DOI: 10.1021/BI00136A006
Page generated: Wed Oct 28 14:15:44 2020
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