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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

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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

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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

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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

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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: Mon Jul 14 04:32:44 2025

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