Atomistry » Copper » PDB 2cj3-2foy » 2e86
Atomistry »
  Copper »
    PDB 2cj3-2foy »
      2e86 »

Copper in PDB 2e86: Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6

Enzymatic activity of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6

All present enzymatic activity of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6:
1.7.2.1;

Protein crystallography data

The structure of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6, PDB code: 2e86 was solved by E.I.Tocheva, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.750, 102.582, 146.000, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 17.9

Copper Binding Sites:

The binding sites of Copper atom in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 (pdb code 2e86). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6, PDB code: 2e86:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 1 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:8.7
occ:1.00
 ND1 A:HIS145 2.1 8.0 1.0
ND1 A:HIS95 2.1 7.0 1.0
SG A:CYS136 2.2 8.1 1.0
SD A:MET150 2.5 7.6 1.0
CE1 A:HIS145 2.9 8.3 1.0
CE1 A:HIS95 3.0 7.5 1.0
CG A:HIS95 3.1 8.1 1.0
CG A:HIS145 3.1 7.5 1.0
CB A:CYS136 3.2 7.5 1.0
CE A:MET150 3.2 8.6 1.0
CB A:HIS95 3.5 7.9 1.0
CB A:HIS145 3.5 7.2 1.0
CG A:MET150 3.8 7.2 1.0
CA A:HIS95 3.9 8.0 1.0
NE2 A:HIS145 4.1 8.4 1.0
NE2 A:HIS95 4.2 7.8 1.0
CD2 A:HIS145 4.2 8.3 1.0
CD2 A:HIS95 4.2 7.5 1.0
CB A:MET150 4.3 6.8 1.0
CG A:PRO138 4.3 9.0 1.0
O A:MET94 4.3 8.9 1.0
SD A:MET62 4.4 9.8 1.0
CA A:CYS136 4.6 7.4 1.0
CD A:PRO138 4.6 8.5 1.0
N A:ASN96 4.7 8.1 1.0
CB A:MET62 4.7 9.3 1.0
CA A:HIS145 4.8 7.2 1.0
C A:HIS95 4.9 8.1 1.0
N A:HIS95 4.9 8.1 1.0

Copper binding site 2 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 2 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:8.7
occ:1.00
 N3 A:AZI503 2.0 24.0 1.0
NE2 A:HIS100 2.0 6.5 1.0
NE2 A:HIS135 2.0 7.2 1.0
NE2 B:HIS306 2.1 7.5 1.0
N2 A:AZI503 2.7 24.0 1.0
CE1 A:HIS100 2.9 6.5 1.0
CD2 A:HIS135 3.0 6.4 1.0
CE1 B:HIS306 3.0 7.4 1.0
CE1 A:HIS135 3.1 6.8 1.0
CD2 A:HIS100 3.1 6.9 1.0
CD2 B:HIS306 3.1 7.7 1.0
OD1 A:ASP98 3.6 13.8 1.0
N1 A:AZI503 3.7 24.1 1.0
ND1 A:HIS100 4.1 6.7 1.0
ND1 B:HIS306 4.1 7.1 1.0
CG A:HIS135 4.1 6.6 1.0
ND1 A:HIS135 4.1 6.7 1.0
NE2 B:HIS255 4.2 9.9 1.0
CG A:HIS100 4.2 7.2 1.0
CG B:HIS306 4.2 7.4 1.0
CG A:ASP98 4.3 10.0 1.0
CE1 B:HIS255 4.4 10.3 1.0
CD2 B:HIS255 4.6 9.7 1.0
OD2 A:ASP98 4.7 10.5 1.0
ND1 B:HIS255 4.8 10.1 1.0
CD2 B:LEU308 4.8 7.9 1.0
O B:HOH2233 4.9 10.6 1.0
CG B:HIS255 4.9 8.7 1.0
CD1 B:LEU308 5.0 8.0 1.0

Copper binding site 3 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 3 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:10.4
occ:1.00
 ND1 B:HIS95 2.1 9.2 1.0
ND1 B:HIS145 2.1 10.2 1.0
SG B:CYS136 2.2 9.6 1.0
SD B:MET150 2.5 8.8 1.0
CE1 B:HIS95 3.0 9.5 1.0
CE1 B:HIS145 3.0 10.1 1.0
CG B:HIS95 3.1 10.3 1.0
CB B:CYS136 3.1 9.6 1.0
CG B:HIS145 3.2 9.5 1.0
CE B:MET150 3.2 9.9 1.0
CB B:HIS95 3.5 10.8 1.0
CB B:HIS145 3.6 9.5 1.0
CA B:HIS95 3.9 10.8 1.0
CG B:MET150 3.9 8.2 1.0
NE2 B:HIS95 4.1 9.6 1.0
NE2 B:HIS145 4.1 10.8 1.0
CG B:PRO138 4.2 11.3 1.0
CD2 B:HIS95 4.2 10.0 1.0
CD2 B:HIS145 4.3 10.4 1.0
O B:MET94 4.3 11.3 1.0
SD B:MET62 4.4 11.4 1.0
CB B:MET150 4.4 8.2 1.0
CA B:CYS136 4.6 9.3 1.0
CD B:PRO138 4.6 11.1 1.0
N B:ASN96 4.7 10.8 1.0
CB B:MET62 4.8 10.4 1.0
CA B:HIS145 4.8 9.4 1.0
C B:HIS95 4.9 10.9 1.0
N B:HIS95 4.9 10.9 1.0
C B:MET94 5.0 11.3 1.0

Copper binding site 4 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 4 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:10.6
occ:1.00
 NE2 B:HIS135 2.0 8.9 1.0
NE2 B:HIS100 2.0 8.6 1.0
NE2 C:HIS306 2.1 8.4 1.0
N3 C:AZI2013 2.1 31.3 1.0
N2 C:AZI2013 2.8 31.3 1.0
CE1 B:HIS100 2.9 8.7 1.0
CD2 B:HIS135 3.0 8.9 1.0
CE1 C:HIS306 3.0 8.7 1.0
CE1 B:HIS135 3.1 8.9 1.0
CD2 B:HIS100 3.1 8.8 1.0
CD2 C:HIS306 3.1 8.4 1.0
OD1 B:ASP98 3.6 15.1 1.0
N1 C:AZI2013 3.8 31.6 1.0
ND1 B:HIS100 4.1 8.2 1.0
NE2 C:HIS255 4.1 11.6 1.0
CG B:HIS135 4.1 8.5 1.0
ND1 C:HIS306 4.1 8.1 1.0
ND1 B:HIS135 4.1 8.7 1.0
CG B:HIS100 4.2 9.3 1.0
CG C:HIS306 4.2 8.4 1.0
CG B:ASP98 4.3 12.0 1.0
CE1 C:HIS255 4.4 11.9 1.0
CD2 C:HIS255 4.5 11.8 1.0
O B:HOH2397 4.6 30.8 1.0
OD2 B:ASP98 4.8 12.4 1.0
ND1 C:HIS255 4.8 12.1 1.0
O C:HOH2206 4.9 11.8 1.0
CG C:HIS255 4.9 10.4 1.0
CD2 C:LEU308 5.0 8.9 1.0
CD1 C:LEU308 5.0 9.7 1.0

Copper binding site 5 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 5 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu501

b:13.9
occ:1.00
 ND1 C:HIS95 2.1 13.6 1.0
ND1 C:HIS145 2.1 13.9 1.0
SG C:CYS136 2.2 12.5 1.0
SD C:MET150 2.5 12.3 1.0
CE1 C:HIS145 3.0 13.5 1.0
CE1 C:HIS95 3.0 14.0 1.0
CG C:HIS95 3.1 14.2 1.0
CB C:CYS136 3.1 11.8 1.0
CG C:HIS145 3.2 12.8 1.0
CE C:MET150 3.3 13.1 1.0
CB C:HIS95 3.5 14.3 1.0
CB C:HIS145 3.5 12.0 1.0
CA C:HIS95 3.9 14.2 1.0
CG C:MET150 3.9 12.0 1.0
NE2 C:HIS145 4.2 14.2 1.0
NE2 C:HIS95 4.2 13.5 1.0
CD2 C:HIS95 4.2 14.2 1.0
CD2 C:HIS145 4.2 13.4 1.0
CG C:PRO138 4.2 13.6 1.0
O C:MET94 4.3 15.4 1.0
CB C:MET150 4.4 11.6 1.0
SD C:MET62 4.4 14.0 1.0
CA C:CYS136 4.6 11.8 1.0
CD C:PRO138 4.6 13.2 1.0
N C:ASN96 4.7 13.7 1.0
CB C:MET62 4.7 13.9 1.0
CA C:HIS145 4.8 11.8 1.0
C C:HIS95 4.8 14.2 1.0
N C:HIS95 4.9 14.8 1.0
C C:MET94 5.0 15.5 1.0

Copper binding site 6 out of 6 in 2e86

Go back to Copper Binding Sites List in 2e86
Copper binding site 6 out of 6 in the Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Azide Bound to Copper Containing Nitrite Reductase From A. Faecalis S- 6 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu502

b:11.6
occ:1.00
 NE2 C:HIS100 2.0 11.6 1.0
NE2 C:HIS135 2.0 10.6 1.0
NE2 A:HIS306 2.1 8.7 1.0
N3 C:AZI503 2.1 26.7 1.0
CE1 C:HIS100 2.9 11.1 1.0
N2 C:AZI503 2.9 26.9 1.0
CD2 C:HIS135 3.0 10.6 1.0
CE1 A:HIS306 3.0 9.6 1.0
CE1 C:HIS135 3.1 10.5 1.0
CD2 C:HIS100 3.1 10.7 1.0
CD2 A:HIS306 3.2 9.7 1.0
OD1 C:ASP98 3.6 16.7 1.0
N1 C:AZI503 3.9 26.6 1.0
ND1 C:HIS100 4.1 10.6 1.0
ND1 A:HIS306 4.1 9.3 1.0
NE2 A:HIS255 4.1 11.5 1.0
CG C:HIS135 4.1 10.4 1.0
ND1 C:HIS135 4.1 10.6 1.0
CG C:HIS100 4.2 10.7 1.0
CG A:HIS306 4.2 9.1 1.0
CE1 A:HIS255 4.3 12.3 1.0
CG C:ASP98 4.4 13.9 1.0
O C:HOH2336 4.5 31.5 1.0
CD2 A:HIS255 4.5 11.5 1.0
ND1 A:HIS255 4.8 11.6 1.0
OD2 C:ASP98 4.9 14.8 1.0
O A:HOH2247 4.9 13.3 1.0
CG A:HIS255 4.9 10.4 1.0
CD2 A:LEU308 4.9 10.5 1.0
CD1 A:LEU308 4.9 11.2 1.0

Reference:

E.I.Tocheva, L.D.Eltis, M.E.P.Murphy. Conserved Active Site Residues Limit Inhibition of A Copper-Containing Nitrite Reductase By Small Molecules. Biochemistry V. 47 4452 2008.
ISSN: ISSN 0006-2960
PubMed: 18358002
DOI: 10.1021/BI7020537
Page generated: Tue Jul 30 23:25:25 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy