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Copper in PDB 1w6c: Agao Holoenzyme in A Small Cell, at 2.2 Angstroms

Enzymatic activity of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms

All present enzymatic activity of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms:
1.4.3.6;

Protein crystallography data

The structure of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms, PDB code: 1w6c was solved by A.P.Duff, D.B.Langley, G.A.Juda, E.M.Shepard, D.M.Dooley, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.16 / 2.20
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 158.041, 64.061, 69.693, 90.00, 111.74, 90.00
R / Rfree (%) 17.2 / 21.9

Other elements in 1w6c:

The structure of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms also contains other interesting chemical elements:

Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms (pdb code 1w6c). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms, PDB code: 1w6c:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1w6c

Go back to Copper Binding Sites List in 1w6c
Copper binding site 1 out of 2 in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:28.8
occ:1.00
NE2 A:HIS433 2.1 16.8 1.0
NE2 A:HIS431 2.1 15.8 1.0
ND1 A:HIS592 2.1 18.7 1.0
O A:HOH2081 2.5 36.5 1.0
CD2 A:HIS433 2.9 21.9 1.0
CD2 A:HIS431 3.0 14.2 1.0
HD2 A:HIS433 3.0 20.1 1.0
HD2 A:HIS431 3.0 15.5 1.0
HB2 A:HIS592 3.1 18.6 1.0
CG A:HIS592 3.1 18.0 1.0
CE1 A:HIS433 3.2 17.4 1.0
CE1 A:HIS592 3.2 21.0 1.0
HB3 A:HIS592 3.2 18.6 1.0
CE1 A:HIS431 3.2 16.1 1.0
O A:HOH2133 3.2 52.5 1.0
CB A:HIS592 3.3 20.8 1.0
HE1 A:HIS592 3.4 20.1 1.0
HE1 A:HIS433 3.4 18.6 1.0
HE1 A:HIS431 3.4 15.4 1.0
HE3 A:MET602 4.1 34.3 1.0
CG A:HIS433 4.1 19.8 1.0
CG A:HIS431 4.1 18.2 1.0
ND1 A:HIS433 4.2 23.5 1.0
ND1 A:HIS431 4.2 13.8 1.0
O A:HOH2074 4.2 41.1 1.0
CD2 A:HIS592 4.2 23.4 1.0
NE2 A:HIS592 4.3 19.7 1.0
O A:HOH2045 4.5 27.9 1.0
HG3 A:PRO594 4.7 20.6 1.0
CA A:HIS592 4.8 17.6 1.0
CE A:MET602 4.9 33.6 1.0
SD A:MET602 4.9 35.8 1.0

Copper binding site 2 out of 2 in 1w6c

Go back to Copper Binding Sites List in 1w6c
Copper binding site 2 out of 2 in the Agao Holoenzyme in A Small Cell, at 2.2 Angstroms


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Agao Holoenzyme in A Small Cell, at 2.2 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:27.7
occ:0.30
NE2 A:HIS170 2.0 26.4 1.0
OD2 A:ASP161 2.1 32.9 1.0
OD2 A:ASP165 2.3 20.6 1.0
OD1 A:ASP165 2.9 23.5 1.0
CE1 A:HIS170 2.9 25.5 1.0
CG A:ASP165 3.0 24.6 1.0
HE1 A:HIS170 3.0 25.5 1.0
CD2 A:HIS170 3.1 18.7 1.0
HB3 A:HIS201 3.1 30.9 1.0
CG A:ASP161 3.2 34.8 1.0
HB2 A:ASP161 3.2 31.5 1.0
HD2 A:HIS170 3.3 21.3 1.0
HA A:HIS201 3.4 29.1 1.0
O A:HOH2016 3.4 26.2 1.0
HB2 A:HIS201 3.5 30.9 1.0
CB A:HIS201 3.6 30.1 1.0
CB A:ASP161 3.7 32.5 1.0
H A:ASP161 3.9 28.5 1.0
CA A:HIS201 3.9 28.8 1.0
ND1 A:HIS170 4.0 25.1 1.0
CG A:HIS170 4.1 22.4 1.0
OD1 A:ASP161 4.2 29.4 1.0
HE1 A:PHE162 4.3 32.8 1.0
HB3 A:ASP161 4.4 31.5 1.0
N A:HIS201 4.4 28.4 1.0
CB A:ASP165 4.4 27.1 1.0
HB2 A:ALA169 4.6 27.2 1.0
N A:ASP161 4.6 27.7 1.0
H A:HIS201 4.7 28.6 1.0
HB2 A:ASP165 4.7 25.6 1.0
HB3 A:ASP165 4.8 25.6 1.0
CA A:ASP161 4.8 30.3 1.0
CE1 A:PHE162 4.8 33.7 1.0
O A:ALA199 4.9 28.1 1.0
O A:GLU200 4.9 28.4 1.0
C A:GLU200 5.0 28.9 1.0

Reference:

D.B.Langley, A.P.Duff, H.C.Freeman, J.M.Guss. The Copper Containing Amine Oxidase From Arthrobacter Globiformis: Refinement at 1.55 and 2.20 A Resolution in Two Crystal Forms. Acta Crystallogr.,Sect.F V. 62 1052 2006.
ISSN: ESSN 1744-3091
PubMed: 17077478
DOI: 10.1107/S1744309106038814
Page generated: Sun Dec 13 11:02:41 2020

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