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Copper in PDB 1l9o: Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis

Enzymatic activity of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis

All present enzymatic activity of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis:
1.7.99.3;

Protein crystallography data

The structure of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis, PDB code: 1l9o was solved by M.J.Boulanger, M.E.P.Murphy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 61.990, 102.350, 146.170, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 19.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis (pdb code 1l9o). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis, PDB code: 1l9o:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6;

Copper binding site 1 out of 6 in 1l9o

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Copper binding site 1 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


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 Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:15.3
occ:1.00
 ND1 A:HIS145 2.0 10.5 1.0
ND1 A:HIS95 2.0 12.6 1.0
SG A:CYS136 2.2 12.6 1.0
SD A:MET150 2.5 13.1 1.0
CE1 A:HIS145 2.8 9.2 1.0
CE1 A:HIS95 3.0 13.0 1.0
CG A:HIS95 3.1 11.0 1.0
CG A:HIS145 3.1 11.0 1.0
CB A:CYS136 3.2 10.2 1.0
CE A:MET150 3.3 13.9 1.0
CB A:HIS95 3.5 10.7 1.0
CB A:HIS145 3.6 10.7 1.0
CA A:HIS95 3.8 11.7 1.0
CG A:MET150 3.9 9.2 1.0
NE2 A:HIS145 4.0 13.6 1.0
NE2 A:HIS95 4.1 12.4 1.0
CD2 A:HIS145 4.1 12.0 1.0
CD2 A:HIS95 4.2 13.2 1.0
CG A:PRO138 4.3 15.1 1.0
SD A:MET62 4.3 14.0 1.0
CB A:MET150 4.3 9.2 1.0
O A:MET94 4.4 13.3 1.0
N A:ASN96 4.6 13.1 1.0
CA A:CYS136 4.6 12.1 1.0
CB A:MET62 4.7 14.7 1.0
CD A:PRO138 4.7 14.6 1.0
CA A:HIS145 4.7 10.8 1.0
C A:HIS95 4.8 12.1 1.0
N A:HIS95 4.9 12.3 1.0

Copper binding site 2 out of 6 in 1l9o

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Copper binding site 2 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


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 Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:16.6
occ:1.00
 O1 B:NO2504 1.9 22.3 1.0
NE2 A:HIS100 2.0 12.1 1.0
NE2 A:HIS135 2.1 13.1 1.0
O A:HOH5294 2.1 20.7 1.0
NE2 B:HIS306 2.1 13.7 1.0
CE1 A:HIS100 2.9 13.7 1.0
CD2 A:HIS135 3.0 12.8 1.0
CD2 B:HIS306 3.1 12.5 1.0
CE1 A:HIS135 3.1 13.5 1.0
CE1 B:HIS306 3.1 12.0 1.0
CD2 A:HIS100 3.1 12.0 1.0
N B:NO2504 3.3 28.3 1.0
O2 B:NO2504 3.6 30.5 1.0
NE2 B:HIS255 3.6 18.0 1.0
CD2 B:HIS255 3.8 17.0 1.0
OD2 A:ASP98 3.9 18.5 1.0
ND1 A:HIS100 4.1 12.1 1.0
ND1 A:HIS135 4.2 11.1 1.0
CG A:HIS135 4.2 11.0 1.0
CG A:HIS100 4.2 10.4 1.0
ND1 B:HIS306 4.2 12.4 1.0
CG B:HIS306 4.2 12.2 1.0
CE1 B:HIS255 4.3 18.4 1.0
CG A:ASP98 4.4 15.3 1.0
CG B:HIS255 4.5 14.0 1.0
OD1 A:ASP98 4.7 13.4 1.0
O A:HOH6001 4.8 13.5 1.0
ND1 B:HIS255 4.8 16.0 1.0

Copper binding site 3 out of 6 in 1l9o

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Copper binding site 3 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu501

b:18.8
occ:1.00
 ND1 B:HIS145 2.0 16.3 1.0
ND1 B:HIS95 2.1 14.6 1.0
SG B:CYS136 2.2 16.0 1.0
SD B:MET150 2.5 15.2 1.0
CE1 B:HIS145 2.9 17.8 1.0
CE1 B:HIS95 3.0 15.5 1.0
CG B:HIS95 3.1 13.9 1.0
CG B:HIS145 3.1 17.5 1.0
CB B:CYS136 3.2 15.2 1.0
CE B:MET150 3.2 14.0 1.0
CB B:HIS95 3.4 16.5 1.0
CB B:HIS145 3.5 15.7 1.0
CA B:HIS95 3.8 14.6 1.0
CG B:MET150 3.9 13.0 1.0
NE2 B:HIS145 4.0 16.3 1.0
CG B:PRO138 4.1 18.9 1.0
NE2 B:HIS95 4.2 14.4 1.0
CD2 B:HIS145 4.2 18.3 1.0
CD2 B:HIS95 4.2 15.1 1.0
SD B:MET62 4.3 16.7 1.0
O B:MET94 4.3 17.9 1.0
CB B:MET150 4.4 13.3 1.0
CD B:PRO138 4.6 17.8 1.0
CA B:CYS136 4.6 14.8 1.0
N B:ASN96 4.6 14.3 1.0
CB B:MET62 4.8 14.2 1.0
CA B:HIS145 4.8 14.4 1.0
C B:HIS95 4.8 16.5 1.0
N B:HIS95 4.9 16.7 1.0

Copper binding site 4 out of 6 in 1l9o

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Copper binding site 4 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu502

b:19.2
occ:1.00
 O1 C:NO2604 2.0 26.5 1.0
NE2 B:HIS100 2.0 12.9 1.0
NE2 B:HIS135 2.1 14.4 1.0
O C:HOH5292 2.1 23.6 1.0
NE2 C:HIS306 2.1 14.5 1.0
CE1 B:HIS100 2.9 14.3 1.0
CD2 B:HIS135 3.1 14.1 1.0
CD2 B:HIS100 3.1 12.8 1.0
CD2 C:HIS306 3.1 15.3 1.0
CE1 B:HIS135 3.1 14.7 1.0
N C:NO2604 3.1 30.5 1.0
CE1 C:HIS306 3.2 15.6 1.0
O2 C:NO2604 3.4 34.7 1.0
NE2 C:HIS255 3.6 17.9 1.0
CD2 C:HIS255 3.8 18.1 1.0
OD2 B:ASP98 3.9 20.7 1.0
O C:HOH5612 4.0 51.6 1.0
ND1 B:HIS100 4.1 13.9 1.0
CG B:HIS100 4.2 12.3 1.0
ND1 B:HIS135 4.2 14.0 1.0
CG B:HIS135 4.2 13.8 1.0
ND1 C:HIS306 4.2 13.3 1.0
CE1 C:HIS255 4.2 16.8 1.0
CG C:HIS306 4.3 15.1 1.0
CG B:ASP98 4.4 16.9 1.0
CG C:HIS255 4.5 16.8 1.0
OD1 B:ASP98 4.7 15.8 1.0
ND1 C:HIS255 4.8 17.8 1.0
O B:HOH6003 4.9 17.9 1.0

Copper binding site 5 out of 6 in 1l9o

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Copper binding site 5 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu501

b:22.1
occ:1.00
 ND1 C:HIS145 2.0 19.4 1.0
ND1 C:HIS95 2.1 18.1 1.0
SG C:CYS136 2.2 20.4 1.0
SD C:MET150 2.4 20.3 1.0
CE1 C:HIS145 2.9 21.1 1.0
CE1 C:HIS95 3.0 21.4 1.0
CG C:HIS145 3.1 20.4 1.0
CG C:HIS95 3.1 20.1 1.0
CB C:CYS136 3.2 19.6 1.0
CE C:MET150 3.2 20.2 1.0
CB C:HIS95 3.5 19.4 1.0
CB C:HIS145 3.5 17.8 1.0
CG C:MET150 3.8 17.1 1.0
CA C:HIS95 3.9 20.4 1.0
NE2 C:HIS145 4.1 20.2 1.0
NE2 C:HIS95 4.2 18.8 1.0
CD2 C:HIS145 4.2 19.6 1.0
CG C:PRO138 4.2 22.0 1.0
CD2 C:HIS95 4.2 20.3 1.0
O C:MET94 4.3 21.8 1.0
CB C:MET150 4.3 17.4 1.0
SD C:MET62 4.4 20.7 1.0
N C:ASN96 4.6 19.2 1.0
CA C:CYS136 4.6 18.7 1.0
CB C:MET62 4.7 20.6 1.0
CD C:PRO138 4.7 20.4 1.0
CA C:HIS145 4.8 17.8 1.0
C C:HIS95 4.8 20.2 1.0
N C:HIS95 4.9 20.4 1.0

Copper binding site 6 out of 6 in 1l9o

Go back to Copper Binding Sites List in 1l9o
Copper binding site 6 out of 6 in the Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Crystal Structure of Nitrite Soaked I257A Variant of the Copper-Containing Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Cu502

b:20.0
occ:1.00
 O1 A:NO2704 1.9 26.3 1.0
NE2 C:HIS100 2.1 15.9 1.0
O A:HOH5295 2.1 26.6 1.0
NE2 A:HIS306 2.1 14.8 1.0
NE2 C:HIS135 2.2 16.8 1.0
CE1 C:HIS100 2.9 17.3 1.0
CE1 A:HIS306 3.1 14.9 1.0
N A:NO2704 3.1 31.6 1.0
CD2 C:HIS135 3.1 17.4 1.0
CD2 A:HIS306 3.1 14.9 1.0
CD2 C:HIS100 3.2 16.2 1.0
CE1 C:HIS135 3.2 16.8 1.0
O2 A:NO2704 3.4 32.7 1.0
NE2 A:HIS255 3.6 22.3 1.0
CD2 A:HIS255 3.7 20.1 1.0
OD2 C:ASP98 3.9 24.4 1.0
ND1 C:HIS100 4.1 17.5 1.0
ND1 A:HIS306 4.2 14.8 1.0
CG C:HIS100 4.2 16.0 1.0
CG A:HIS306 4.3 14.2 1.0
CG C:HIS135 4.3 16.6 1.0
ND1 C:HIS135 4.3 18.0 1.0
CE1 A:HIS255 4.3 20.9 1.0
CG C:ASP98 4.5 21.5 1.0
CG A:HIS255 4.5 18.6 1.0
OD1 C:ASP98 4.8 18.9 1.0
ND1 A:HIS255 4.8 19.6 1.0
O C:HOH6005 4.8 15.3 1.0

Reference:

M.J.Boulanger, M.E.P.Murphy. Directing the Mode of Nitrite Binding to A Copper-Containing Nitrite Reductase From Alcaligenes Faecalis S-6: Characterization of An Active Site Isoleucine Protein Sci. V. 12 248 2003.
ISSN: ISSN 0961-8368
PubMed: 12538888
DOI: 10.1110/PS.0224503
Page generated: Tue Jul 30 22:12:51 2024

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