Copper in PDB 5f7a: Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Enzymatic activity of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
All present enzymatic activity of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K:
1.7.2.1;
Protein crystallography data
The structure of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K, PDB code: 5f7a
was solved by
Y.Fukuda,
K.M.Tse,
T.Nakane,
T.Nakatsu,
M.Suzuki,
M.Sugahara,
S.Inoue,
T.Masuda,
F.Yumoto,
N.Matsugaki,
E.Nango,
K.Tono,
Y.Joti,
T.Kameshima,
C.Song,
T.Hatsui,
M.Yabashi,
O.Nureki,
M.E.P.Murphy,
T.Inoue,
S.Iwata,
E.Mizohata,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
48.89 /
1.54
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
62.860,
103.686,
146.972,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
15.1 /
18
|
Copper Binding Sites:
The binding sites of Copper atom in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
(pdb code 5f7a). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K, PDB code: 5f7a:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 1 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu501
b:20.3
occ:1.00
|
ND1
|
A:HIS145
|
1.9
|
19.6
|
1.0
|
ND1
|
A:HIS95
|
2.0
|
18.1
|
1.0
|
SG
|
A:CYS136
|
2.1
|
18.9
|
1.0
|
SD
|
A:MET150
|
2.5
|
20.1
|
1.0
|
CE1
|
A:HIS145
|
2.8
|
19.6
|
1.0
|
CE1
|
A:HIS95
|
3.0
|
18.7
|
1.0
|
CG
|
A:HIS145
|
3.0
|
18.8
|
1.0
|
CG
|
A:HIS95
|
3.1
|
19.0
|
1.0
|
CB
|
A:CYS136
|
3.2
|
17.7
|
1.0
|
CE
|
A:MET150
|
3.3
|
20.8
|
1.0
|
CB
|
A:HIS95
|
3.4
|
18.9
|
1.0
|
CB
|
A:HIS145
|
3.5
|
18.7
|
1.0
|
CA
|
A:HIS95
|
3.8
|
19.2
|
1.0
|
CG
|
A:MET150
|
3.9
|
15.9
|
1.0
|
NE2
|
A:HIS145
|
4.0
|
20.4
|
1.0
|
CD2
|
A:HIS145
|
4.1
|
18.5
|
1.0
|
NE2
|
A:HIS95
|
4.1
|
21.4
|
1.0
|
CD2
|
A:HIS95
|
4.2
|
19.3
|
1.0
|
O
|
A:MET94
|
4.2
|
20.8
|
0.2
|
O
|
A:MET94
|
4.2
|
20.6
|
0.8
|
CG
|
A:PRO138
|
4.3
|
24.8
|
1.0
|
CB
|
A:MET150
|
4.4
|
16.7
|
1.0
|
SD
|
A:MET62
|
4.4
|
22.3
|
1.0
|
CA
|
A:CYS136
|
4.6
|
16.3
|
1.0
|
N
|
A:ASN96
|
4.6
|
20.3
|
1.0
|
CA
|
A:HIS145
|
4.7
|
17.4
|
1.0
|
CD
|
A:PRO138
|
4.7
|
20.4
|
1.0
|
CB
|
A:MET62
|
4.8
|
20.7
|
1.0
|
C
|
A:HIS95
|
4.8
|
21.2
|
1.0
|
N
|
A:HIS95
|
4.8
|
21.2
|
1.0
|
C
|
A:MET94
|
4.9
|
19.9
|
0.8
|
C
|
A:MET94
|
4.9
|
21.1
|
0.2
|
|
Copper binding site 2 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 2 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu502
b:17.2
occ:1.00
|
NE2
|
A:HIS100
|
2.0
|
15.8
|
1.0
|
NE2
|
C:HIS306
|
2.0
|
14.7
|
1.0
|
NE2
|
A:HIS135
|
2.0
|
16.9
|
1.0
|
O2
|
A:NO2503
|
2.1
|
30.8
|
1.0
|
O1
|
A:NO2503
|
2.1
|
20.5
|
1.0
|
N
|
A:NO2503
|
2.3
|
25.4
|
1.0
|
CE1
|
A:HIS100
|
2.9
|
16.3
|
1.0
|
CD2
|
A:HIS100
|
3.0
|
16.1
|
1.0
|
CD2
|
C:HIS306
|
3.0
|
16.8
|
1.0
|
CE1
|
C:HIS306
|
3.0
|
14.6
|
1.0
|
CD2
|
A:HIS135
|
3.0
|
17.7
|
1.0
|
CE1
|
A:HIS135
|
3.0
|
17.4
|
1.0
|
OD2
|
A:ASP98
|
3.9
|
29.8
|
1.0
|
ND1
|
A:HIS100
|
4.1
|
16.7
|
1.0
|
NE2
|
C:HIS255
|
4.1
|
19.1
|
1.0
|
CG
|
A:HIS100
|
4.1
|
16.6
|
1.0
|
ND1
|
C:HIS306
|
4.1
|
14.2
|
1.0
|
CG
|
C:HIS306
|
4.2
|
14.2
|
1.0
|
ND1
|
A:HIS135
|
4.2
|
16.1
|
1.0
|
CG
|
A:HIS135
|
4.2
|
16.5
|
1.0
|
CD2
|
C:HIS255
|
4.3
|
17.8
|
1.0
|
CE1
|
C:HIS255
|
4.5
|
21.4
|
1.0
|
CG
|
A:ASP98
|
4.6
|
22.7
|
1.0
|
CG
|
C:HIS255
|
4.8
|
15.0
|
1.0
|
OD1
|
A:ASP98
|
4.9
|
22.5
|
1.0
|
O
|
C:HOH719
|
4.9
|
23.4
|
1.0
|
ND1
|
C:HIS255
|
4.9
|
20.6
|
1.0
|
CD2
|
C:LEU308
|
4.9
|
18.5
|
1.0
|
|
Copper binding site 3 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 3 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu504
b:18.3
occ:1.00
|
NE2
|
A:HIS306
|
2.0
|
14.9
|
1.0
|
NE2
|
B:HIS100
|
2.0
|
16.0
|
1.0
|
O2
|
A:NO2505
|
2.0
|
32.5
|
1.0
|
NE2
|
B:HIS135
|
2.1
|
18.1
|
1.0
|
O1
|
A:NO2505
|
2.1
|
23.2
|
1.0
|
N
|
A:NO2505
|
2.3
|
27.7
|
1.0
|
CE1
|
A:HIS306
|
2.9
|
16.1
|
1.0
|
CE1
|
B:HIS100
|
2.9
|
15.7
|
1.0
|
CD2
|
A:HIS306
|
3.0
|
16.5
|
1.0
|
CE1
|
B:HIS135
|
3.0
|
17.6
|
1.0
|
CD2
|
B:HIS100
|
3.1
|
16.8
|
1.0
|
CD2
|
B:HIS135
|
3.1
|
16.9
|
1.0
|
OD2
|
B:ASP98
|
4.0
|
29.2
|
1.0
|
NE2
|
A:HIS255
|
4.0
|
21.2
|
1.0
|
ND1
|
A:HIS306
|
4.1
|
14.8
|
1.0
|
ND1
|
B:HIS100
|
4.1
|
15.6
|
1.0
|
CG
|
B:HIS100
|
4.1
|
15.6
|
1.0
|
CG
|
A:HIS306
|
4.1
|
15.2
|
1.0
|
ND1
|
B:HIS135
|
4.2
|
17.7
|
1.0
|
CG
|
B:HIS135
|
4.2
|
16.3
|
1.0
|
CD2
|
A:HIS255
|
4.3
|
22.4
|
1.0
|
CE1
|
A:HIS255
|
4.5
|
22.8
|
1.0
|
CG
|
B:ASP98
|
4.6
|
23.6
|
1.0
|
OD1
|
B:ASP98
|
4.7
|
24.5
|
1.0
|
CG
|
A:HIS255
|
4.9
|
19.5
|
1.0
|
ND1
|
A:HIS255
|
4.9
|
22.5
|
1.0
|
O
|
A:HOH672
|
4.9
|
23.3
|
1.0
|
CD2
|
A:LEU308
|
5.0
|
21.8
|
1.0
|
|
Copper binding site 4 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 4 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu501
b:21.0
occ:1.00
|
ND1
|
B:HIS145
|
1.9
|
17.5
|
1.0
|
ND1
|
B:HIS95
|
2.0
|
20.3
|
1.0
|
SG
|
B:CYS136
|
2.2
|
20.0
|
1.0
|
SD
|
B:MET150
|
2.6
|
20.4
|
1.0
|
CE1
|
B:HIS145
|
2.9
|
20.9
|
1.0
|
CE1
|
B:HIS95
|
3.0
|
18.1
|
1.0
|
CG
|
B:HIS145
|
3.0
|
19.5
|
1.0
|
CG
|
B:HIS95
|
3.0
|
21.0
|
1.0
|
CB
|
B:CYS136
|
3.2
|
18.6
|
1.0
|
CB
|
B:HIS95
|
3.4
|
20.1
|
1.0
|
CE
|
B:MET150
|
3.4
|
23.9
|
1.0
|
CB
|
B:HIS145
|
3.5
|
17.9
|
1.0
|
CA
|
B:HIS95
|
3.8
|
19.4
|
1.0
|
NE2
|
B:HIS145
|
4.0
|
19.9
|
1.0
|
CG
|
B:MET150
|
4.0
|
17.5
|
1.0
|
CD2
|
B:HIS145
|
4.1
|
19.5
|
1.0
|
NE2
|
B:HIS95
|
4.1
|
20.4
|
1.0
|
CD2
|
B:HIS95
|
4.1
|
18.7
|
1.0
|
O
|
B:MET94
|
4.2
|
21.9
|
0.8
|
CG
|
B:PRO138
|
4.2
|
23.4
|
1.0
|
O
|
B:MET94
|
4.4
|
21.3
|
0.2
|
SD
|
B:MET62
|
4.4
|
21.5
|
1.0
|
CB
|
B:MET150
|
4.4
|
17.4
|
1.0
|
N
|
B:ASN96
|
4.6
|
19.5
|
1.0
|
CA
|
B:CYS136
|
4.6
|
19.0
|
1.0
|
CD
|
B:PRO138
|
4.7
|
21.9
|
1.0
|
CA
|
B:HIS145
|
4.7
|
16.8
|
1.0
|
C
|
B:HIS95
|
4.7
|
23.2
|
1.0
|
N
|
B:HIS95
|
4.8
|
24.0
|
1.0
|
CB
|
B:MET62
|
4.9
|
17.5
|
1.0
|
C
|
B:MET94
|
4.9
|
22.2
|
0.8
|
|
Copper binding site 5 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 5 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu502
b:13.6
occ:1.00
|
NE2
|
C:HIS100
|
2.0
|
11.2
|
1.0
|
NE2
|
B:HIS306
|
2.0
|
12.5
|
1.0
|
NE2
|
C:HIS135
|
2.0
|
12.3
|
1.0
|
O2
|
B:NO2503
|
2.1
|
27.4
|
1.0
|
O1
|
B:NO2503
|
2.1
|
19.0
|
1.0
|
N
|
B:NO2503
|
2.3
|
27.8
|
1.0
|
CE1
|
C:HIS100
|
2.9
|
12.5
|
1.0
|
CE1
|
B:HIS306
|
3.0
|
11.8
|
1.0
|
CE1
|
C:HIS135
|
3.0
|
13.2
|
1.0
|
CD2
|
C:HIS100
|
3.0
|
11.8
|
1.0
|
CD2
|
C:HIS135
|
3.0
|
12.2
|
1.0
|
CD2
|
B:HIS306
|
3.1
|
12.7
|
1.0
|
OD2
|
C:ASP98
|
4.0
|
24.6
|
1.0
|
ND1
|
C:HIS100
|
4.0
|
13.2
|
1.0
|
ND1
|
B:HIS306
|
4.1
|
11.3
|
1.0
|
NE2
|
B:HIS255
|
4.1
|
16.8
|
1.0
|
ND1
|
C:HIS135
|
4.1
|
11.5
|
1.0
|
CG
|
C:HIS100
|
4.1
|
11.0
|
1.0
|
CG
|
C:HIS135
|
4.2
|
11.8
|
1.0
|
CG
|
B:HIS306
|
4.2
|
11.7
|
1.0
|
CD2
|
B:HIS255
|
4.4
|
15.3
|
1.0
|
CE1
|
B:HIS255
|
4.5
|
18.6
|
1.0
|
CG
|
C:ASP98
|
4.6
|
20.1
|
1.0
|
OD1
|
C:ASP98
|
4.7
|
18.1
|
1.0
|
O
|
B:HOH694
|
4.9
|
19.0
|
1.0
|
ND1
|
B:HIS255
|
4.9
|
17.9
|
1.0
|
CD2
|
B:LEU308
|
4.9
|
16.0
|
1.0
|
CG
|
B:HIS255
|
4.9
|
13.6
|
1.0
|
|
Copper binding site 6 out
of 6 in 5f7a
Go back to
Copper Binding Sites List in 5f7a
Copper binding site 6 out
of 6 in the Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Nitrite Complex Structure of Copper Nitrite Reductase From Alcaligenes Faecalis Determined at 293 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu501
b:14.6
occ:1.00
|
ND1
|
C:HIS145
|
2.0
|
12.9
|
1.0
|
ND1
|
C:HIS95
|
2.0
|
12.7
|
1.0
|
SG
|
C:CYS136
|
2.2
|
13.8
|
1.0
|
SD
|
C:MET150
|
2.5
|
14.4
|
1.0
|
CE1
|
C:HIS145
|
2.9
|
14.2
|
1.0
|
CE1
|
C:HIS95
|
3.0
|
13.9
|
1.0
|
CG
|
C:HIS95
|
3.0
|
12.9
|
1.0
|
CG
|
C:HIS145
|
3.0
|
13.2
|
1.0
|
CB
|
C:CYS136
|
3.3
|
12.2
|
1.0
|
CE
|
C:MET150
|
3.4
|
15.3
|
1.0
|
CB
|
C:HIS95
|
3.5
|
14.2
|
1.0
|
CB
|
C:HIS145
|
3.5
|
13.2
|
1.0
|
CA
|
C:HIS95
|
3.8
|
13.5
|
1.0
|
CG
|
C:MET150
|
4.0
|
14.2
|
1.0
|
NE2
|
C:HIS145
|
4.1
|
13.7
|
1.0
|
NE2
|
C:HIS95
|
4.1
|
13.4
|
1.0
|
CD2
|
C:HIS145
|
4.1
|
14.0
|
1.0
|
CD2
|
C:HIS95
|
4.2
|
15.1
|
1.0
|
CG
|
C:PRO138
|
4.3
|
18.4
|
1.0
|
O
|
C:MET94
|
4.3
|
16.4
|
1.0
|
CB
|
C:MET150
|
4.4
|
11.6
|
1.0
|
SD
|
C:MET62
|
4.4
|
17.4
|
1.0
|
N
|
C:ASN96
|
4.6
|
13.7
|
1.0
|
CA
|
C:CYS136
|
4.7
|
11.5
|
1.0
|
CD
|
C:PRO138
|
4.7
|
15.3
|
1.0
|
CA
|
C:HIS145
|
4.8
|
12.3
|
1.0
|
C
|
C:HIS95
|
4.8
|
13.8
|
1.0
|
N
|
C:HIS95
|
4.8
|
13.1
|
1.0
|
CB
|
C:MET62
|
4.9
|
14.1
|
1.0
|
C
|
C:MET94
|
5.0
|
16.0
|
1.0
|
|
Reference:
Y.Fukuda,
K.M.Tse,
T.Nakane,
T.Nakatsu,
M.Suzuki,
M.Sugahara,
S.Inoue,
T.Masuda,
F.Yumoto,
N.Matsugaki,
E.Nango,
K.Tono,
Y.Joti,
T.Kameshima,
C.Song,
T.Hatsui,
M.Yabashi,
O.Nureki,
M.E.P.Murphy,
T.Inoue,
S.Iwata,
E.Mizohata.
Redox-Coupled Proton Transfer Mechanism in Nitrite Reductase Revealed By Femtosecond Crystallography Proc.Natl.Acad.Sci.Usa V. 113 2928 2016.
ISSN: ESSN 1091-6490
PubMed: 26929369
DOI: 10.1073/PNAS.1517770113
Page generated: Wed Jul 31 04:04:33 2024
|