Atomistry » Copper » PDB 1oe2-1rjp » 1w6g
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1w6g »

Copper in PDB 1w6g: Agao Holoenzyme at 1.55 Angstroms

Enzymatic activity of Agao Holoenzyme at 1.55 Angstroms

All present enzymatic activity of Agao Holoenzyme at 1.55 Angstroms:
1.4.3.6;

Protein crystallography data

The structure of Agao Holoenzyme at 1.55 Angstroms, PDB code: 1w6g was solved by D.B.Langley, A.P.Duff, 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) 25.82 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.836, 63.243, 91.982, 90.00, 112.03, 90.00
R / Rfree (%) 17 / 18.8

Copper Binding Sites:

The binding sites of Copper atom in the Agao Holoenzyme at 1.55 Angstroms (pdb code 1w6g). 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 at 1.55 Angstroms, PDB code: 1w6g:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1w6g

Go back to Copper Binding Sites List in 1w6g
Copper binding site 1 out of 2 in the Agao Holoenzyme at 1.55 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 at 1.55 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:30.2
occ:1.00
NE2 A:HIS431 2.0 5.5 1.0
ND1 A:HIS592 2.0 11.0 0.8
NE2 A:HIS433 2.1 10.9 1.0
O4 A:TPQ382 2.2 26.8 0.3
ND1 A:HIS592 2.2 6.0 0.2
O A:HOH2292 2.3 37.2 0.7
O A:HOH2293 2.7 31.4 0.7
CE1 A:HIS592 3.0 7.9 0.8
CD2 A:HIS431 3.0 4.6 1.0
CE1 A:HIS431 3.0 5.0 1.0
CD2 A:HIS433 3.0 9.5 1.0
CE1 A:HIS433 3.1 10.3 1.0
CG A:HIS592 3.1 5.3 0.8
HE1 A:HIS592 3.1 7.9 0.8
CG A:HIS592 3.1 6.2 0.2
HB2 A:HIS592 3.1 6.0 0.2
HD2 A:HIS431 3.2 4.7 1.0
CE1 A:HIS592 3.2 3.5 0.2
C4 A:TPQ382 3.2 19.7 0.3
HD2 A:HIS433 3.2 8.9 1.0
HB3 A:HIS592 3.2 6.3 0.8
HE1 A:HIS431 3.2 4.9 1.0
HB2 A:HIS592 3.2 6.3 0.8
HB3 A:HIS592 3.3 6.0 0.2
HE1 A:HIS433 3.3 10.0 1.0
HE1 A:HIS592 3.4 3.9 0.2
CB A:HIS592 3.4 6.5 0.2
CB A:HIS592 3.4 7.8 0.8
O5 A:TPQ382 3.8 9.3 0.3
C5 A:TPQ382 3.9 19.2 0.3
C3 A:TPQ382 4.1 18.6 0.3
ND1 A:HIS431 4.1 4.1 1.0
NE2 A:HIS592 4.1 4.6 0.8
CG A:HIS431 4.1 4.1 1.0
H3 A:TPQ382 4.2 18.6 0.3
ND1 A:HIS433 4.2 8.5 1.0
CG A:HIS433 4.2 5.6 1.0
CD2 A:HIS592 4.2 6.0 0.8
HE3 A:MET602 4.2 27.0 0.5
NE2 A:HIS592 4.3 2.5 0.2
CD2 A:HIS592 4.3 7.7 0.2
HE3 A:MET602 4.4 20.4 0.5
O A:HOH2217 4.4 31.2 1.0
HG3 A:PRO594 4.7 6.2 1.0
SD A:MET602 4.8 32.9 0.5
SD A:MET602 4.8 29.5 0.5
HG11 A:VAL406 4.9 17.5 1.0
CA A:HIS592 4.9 5.7 1.0
CE A:MET602 5.0 24.4 0.5
CE A:MET602 5.0 16.4 0.5

Copper binding site 2 out of 2 in 1w6g

Go back to Copper Binding Sites List in 1w6g
Copper binding site 2 out of 2 in the Agao Holoenzyme at 1.55 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 at 1.55 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu702

b:35.3
occ:0.40
ND1 A:HIS201 1.9 7.7 0.5
NE2 A:HIS170 2.0 10.9 1.0
OD2 A:ASP165 2.3 15.9 1.0
OD2 A:ASP161 2.3 16.0 1.0
HE1 A:HIS201 2.5 11.0 0.5
CE1 A:HIS201 2.6 14.0 0.5
OD1 A:ASP165 2.8 14.8 1.0
CG A:ASP165 2.9 15.0 1.0
CE1 A:HIS170 3.0 12.8 1.0
CD2 A:HIS170 3.0 12.8 1.0
HB2 A:ASP161 3.0 13.1 1.0
HE1 A:HIS170 3.2 11.5 1.0
HD2 A:HIS170 3.2 11.4 1.0
CG A:HIS201 3.2 12.1 0.5
CG A:ASP161 3.2 15.8 1.0
HB3 A:HIS201 3.4 14.1 0.5
HA A:HIS201 3.5 14.7 1.0
O A:HOH2137 3.5 32.5 1.0
HB2 A:HIS201 3.6 14.1 0.5
CB A:ASP161 3.6 13.0 1.0
H A:ASP161 3.8 12.1 1.0
HB3 A:HIS201 3.8 14.2 0.5
NE2 A:HIS201 3.8 7.6 0.5
CB A:HIS201 3.8 14.5 0.5
CB A:HIS201 3.9 14.4 0.5
ND1 A:HIS170 4.1 8.9 1.0
CG A:HIS170 4.1 8.6 1.0
H31 A:GOL752 4.1 49.7 1.0
CD2 A:HIS201 4.1 13.8 0.5
CA A:HIS201 4.1 14.7 1.0
HE1 A:PHE162 4.2 19.0 1.0
HB3 A:ASP161 4.3 13.1 1.0
OD1 A:ASP161 4.3 21.3 1.0
CB A:ASP165 4.3 10.1 1.0
N A:ASP161 4.4 12.3 1.0
HB2 A:ASP165 4.5 11.5 1.0
HB3 A:ALA169 4.6 8.3 1.0
HB3 A:ASP165 4.7 11.5 1.0
CA A:ASP161 4.7 12.5 1.0
CE1 A:PHE162 4.7 19.0 1.0
N A:HIS201 4.7 14.7 1.0
HB2 A:HIS201 4.8 14.2 0.5
O A:ALA199 4.9 14.2 1.0
H A:GLY202 4.9 14.5 1.0
ND2 A:ASN203 5.0 12.5 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: Thu Sep 3 16:23:48 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy