Atomistry » Copper » PDB 1rju-1tl4 » 1snr
Atomistry »
  Copper »
    PDB 1rju-1tl4 »
      1snr »

Copper in PDB 1snr: Nitric Oxide Bound to Cu Nitrite Reductase

Enzymatic activity of Nitric Oxide Bound to Cu Nitrite Reductase

All present enzymatic activity of Nitric Oxide Bound to Cu Nitrite Reductase:
1.7.2.1;

Protein crystallography data

The structure of Nitric Oxide Bound to Cu Nitrite Reductase, PDB code: 1snr was solved by E.I.Tocheva, F.I.Rosell, A.G.Mauk, M.E.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.30 / 1.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.726, 102.595, 145.652, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 14.1

Copper Binding Sites:

The binding sites of Copper atom in the Nitric Oxide Bound to Cu Nitrite Reductase (pdb code 1snr). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Nitric Oxide Bound to Cu Nitrite Reductase, PDB code: 1snr:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 1 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:10.0
occ:1.00
 ND1 A:HIS145 2.1 9.8 1.0
ND1 A:HIS95 2.1 9.4 1.0
SG A:CYS136 2.2 9.7 1.0
SD A:MET150 2.4 9.9 1.0
CE1 A:HIS145 3.0 10.4 1.0
CE1 A:HIS95 3.0 10.3 1.0
CG A:HIS95 3.1 10.1 1.0
CG A:HIS145 3.1 9.2 1.0
CB A:CYS136 3.2 8.9 1.0
CE A:MET150 3.2 10.1 1.0
CB A:HIS95 3.5 9.4 1.0
CB A:HIS145 3.5 8.9 1.0
CG A:MET150 3.8 8.9 1.0
CA A:HIS95 3.8 9.3 1.0
NE2 A:HIS145 4.1 10.3 1.0
NE2 A:HIS95 4.1 10.7 1.0
CD2 A:HIS95 4.2 12.8 1.0
CD2 A:HIS145 4.2 11.5 1.0
CB A:MET150 4.3 8.8 1.0
CG A:PRO138 4.3 10.7 1.0
O A:MET94 4.3 9.4 1.0
SD A:MET62 4.4 11.9 1.0
CA A:CYS136 4.6 8.5 1.0
CD A:PRO138 4.7 9.2 1.0
N A:ASN96 4.7 9.0 1.0
CB A:MET62 4.7 11.1 1.0
CA A:HIS145 4.8 8.6 1.0
C A:HIS95 4.8 8.9 1.0
N A:HIS95 4.9 9.2 1.0

Copper binding site 2 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 2 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:9.9
occ:1.00
 O A:NO503 1.9 25.9 1.0
N A:NO503 2.0 23.4 1.0
NE2 A:HIS100 2.0 9.2 1.0
NE2 B:HIS306 2.0 8.5 1.0
NE2 A:HIS135 2.1 8.1 1.0
CE1 A:HIS100 2.9 8.0 1.0
CE1 B:HIS306 3.0 8.2 1.0
CD2 A:HIS135 3.1 8.0 1.0
CD2 B:HIS306 3.1 9.2 1.0
CD2 A:HIS100 3.1 7.8 1.0
CE1 A:HIS135 3.1 7.9 1.0
OD1 A:ASP98 3.7 18.5 1.0
NE2 B:HIS255 4.0 14.4 1.0
ND1 A:HIS100 4.1 8.2 1.0
ND1 B:HIS306 4.1 8.0 1.0
CG A:HIS100 4.2 7.8 1.0
CE1 B:HIS255 4.2 13.7 1.0
ND1 A:HIS135 4.2 8.0 1.0
CG B:HIS306 4.2 8.2 1.0
CG A:HIS135 4.2 7.7 1.0
CG A:ASP98 4.4 13.8 1.0
CD2 B:HIS255 4.5 12.5 1.0
OD2 A:ASP98 4.7 15.6 1.0
ND1 B:HIS255 4.7 12.2 1.0
CD2 B:LEU308 4.9 9.9 1.0
O B:HOH1726 4.9 16.6 1.0
CG B:HIS255 4.9 9.9 1.0

Copper binding site 3 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 3 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:12.1
occ:1.00
 ND1 B:HIS95 2.1 11.0 1.0
ND1 B:HIS145 2.1 11.2 1.0
SG B:CYS136 2.2 11.9 1.0
SD B:MET150 2.5 11.5 1.0
CE1 B:HIS145 3.0 12.2 1.0
CE1 B:HIS95 3.0 11.3 1.0
CG B:HIS95 3.1 11.6 1.0
CG B:HIS145 3.1 11.0 1.0
CB B:CYS136 3.2 10.8 1.0
CE B:MET150 3.3 11.1 1.0
CB B:HIS95 3.5 11.8 1.0
CB B:HIS145 3.5 10.5 1.0
CA B:HIS95 3.8 12.1 1.0
CG B:MET150 3.9 10.2 1.0
NE2 B:HIS145 4.1 12.5 1.0
NE2 B:HIS95 4.1 11.3 1.0
CG B:PRO138 4.2 12.9 1.0
CD2 B:HIS145 4.2 12.2 1.0
CD2 B:HIS95 4.2 11.9 1.0
O B:MET94 4.3 12.3 1.0
SD B:MET62 4.4 13.8 1.0
CB B:MET150 4.4 9.7 1.0
CD B:PRO138 4.5 11.7 1.0
CA B:CYS136 4.6 10.4 1.0
N B:ASN96 4.7 11.4 1.0
CA B:HIS145 4.8 10.6 1.0
C B:HIS95 4.8 11.9 1.0
N B:HIS95 4.8 12.2 1.0
CB B:MET62 4.8 11.1 1.0
C B:MET94 5.0 12.0 1.0

Copper binding site 4 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 4 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:11.5
occ:1.00
 N B:NO503 2.0 26.3 1.0
NE2 B:HIS100 2.0 10.4 1.0
NE2 B:HIS135 2.1 10.4 1.0
NE2 C:HIS306 2.1 10.1 1.0
O B:NO503 2.1 27.2 1.0
CE1 B:HIS100 3.0 10.3 1.0
CD2 B:HIS135 3.0 10.3 1.0
CE1 C:HIS306 3.0 10.1 1.0
CE1 B:HIS135 3.1 9.5 1.0
CD2 C:HIS306 3.1 10.5 1.0
CD2 B:HIS100 3.1 10.2 1.0
OD1 B:ASP98 3.7 20.4 1.0
NE2 C:HIS255 4.0 15.8 1.0
ND1 B:HIS100 4.1 10.1 1.0
ND1 C:HIS306 4.2 9.4 1.0
ND1 B:HIS135 4.2 10.0 1.0
CG B:HIS135 4.2 9.8 1.0
CG B:HIS100 4.2 10.3 1.0
CG C:HIS306 4.2 9.8 1.0
CE1 C:HIS255 4.2 16.0 1.0
CG B:ASP98 4.3 15.4 1.0
CD2 C:HIS255 4.5 15.1 1.0
OD2 B:ASP98 4.7 17.5 1.0
ND1 C:HIS255 4.7 14.0 1.0
O C:HOH1700 4.9 17.7 1.0
CG C:HIS255 4.9 11.2 1.0
CD2 C:LEU308 5.0 12.7 1.0

Copper binding site 5 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 5 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu501

b:15.2
occ:1.00
 ND1 C:HIS95 2.1 15.7 1.0
ND1 C:HIS145 2.1 14.6 1.0
SG C:CYS136 2.2 14.6 1.0
SD C:MET150 2.5 14.5 1.0
CE1 C:HIS145 3.0 15.2 1.0
CE1 C:HIS95 3.0 14.0 1.0
CG C:HIS95 3.1 14.8 1.0
CG C:HIS145 3.2 13.6 1.0
CB C:CYS136 3.2 13.7 1.0
CE C:MET150 3.3 15.1 1.0
CB C:HIS95 3.5 15.0 1.0
CB C:HIS145 3.6 13.0 1.0
CA C:HIS95 3.8 14.6 1.0
CG C:MET150 3.9 13.6 1.0
NE2 C:HIS95 4.1 15.0 1.0
NE2 C:HIS145 4.1 15.2 1.0
CD2 C:HIS95 4.2 15.7 1.0
CG C:PRO138 4.2 14.9 1.0
CD2 C:HIS145 4.2 14.3 1.0
O C:MET94 4.3 16.1 1.0
CB C:MET150 4.4 12.5 1.0
SD C:MET62 4.5 15.6 1.0
CD C:PRO138 4.6 13.9 1.0
CA C:CYS136 4.6 13.1 1.0
N C:ASN96 4.6 14.2 1.0
CB C:MET62 4.8 14.3 1.0
CA C:HIS145 4.8 12.6 1.0
C C:HIS95 4.8 14.5 1.0
N C:HIS95 4.8 14.9 1.0
C C:MET94 5.0 15.5 1.0

Copper binding site 6 out of 6 in 1snr

Go back to Copper Binding Sites List in 1snr
Copper binding site 6 out of 6 in the Nitric Oxide Bound to Cu Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Nitric Oxide Bound to Cu Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu502

b:12.9
occ:1.00
 N C:NO503 2.0 24.6 1.0
O C:NO503 2.0 26.0 1.0
NE2 C:HIS100 2.0 10.9 1.0
NE2 C:HIS135 2.0 12.4 1.0
NE2 A:HIS306 2.1 10.2 1.0
CE1 C:HIS100 2.9 11.1 1.0
CD2 C:HIS135 3.0 12.8 1.0
CE1 A:HIS306 3.0 11.0 1.0
CE1 C:HIS135 3.1 12.1 1.0
CD2 A:HIS306 3.1 10.6 1.0
CD2 C:HIS100 3.1 11.0 1.0
OD1 C:ASP98 3.8 23.2 1.0
NE2 A:HIS255 4.0 16.4 1.0
ND1 C:HIS100 4.1 11.2 1.0
ND1 A:HIS306 4.1 10.9 1.0
ND1 C:HIS135 4.2 12.0 1.0
CG C:HIS135 4.2 12.6 1.0
CG C:HIS100 4.2 10.7 1.0
CE1 A:HIS255 4.2 16.9 1.0
CG A:HIS306 4.2 10.6 1.0
CG C:ASP98 4.4 18.1 1.0
CD2 A:HIS255 4.5 15.2 1.0
OD2 C:ASP98 4.7 19.3 1.0
ND1 A:HIS255 4.7 14.6 1.0
CG A:HIS255 4.9 11.5 1.0
O A:HOH1750 4.9 19.8 1.0
CD2 A:LEU308 4.9 11.8 1.0

Reference:

E.I.Tocheva, F.I.Rosell, A.G.Mauk, M.E.Murphy. Side-on Copper-Nitrosyl Coordination By Nitrite Reductase. Science V. 304 867 2004.
ISSN: ISSN 0036-8075
PubMed: 15131305
DOI: 10.1126/SCIENCE.1095109
Page generated: Sun Dec 13 11:02:01 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy