Chlorine in PDB 4ysc: Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis

All present enzymatic activity of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis:
1.7.2.1;

The structure of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis, PDB code: 4ysc was solved by Y.Fukuda, K.M.Tse, M.Suzuki, K.Diederichs, K.Hirata, T.Nakane, M.Sugahara, E.Nango, K.Tono, Y.Joti, T.Kameshima, C.Song, T.Hatsui, M.Yabashi, O.Nureki, H.Matsumura, 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)	73.90 / 2.03
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	63.100, 103.800, 147.800, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 20.3

The structure of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis also contains other interesting chemical elements:

Copper

(Cu)

6 atoms

The binding sites of Chlorine atom in the Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis (pdb code 4ysc). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis, PDB code: 4ysc:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:38.1 occ:1.00 CU A:CU402 2.2 33.7 1.0 NE2 C:HIS306 3.1 30.6 1.0 NE2 A:HIS135 3.2 30.3 1.0 CD1 C:ILE257 3.4 31.7 1.0 CE1 A:HIS135 3.5 27.8 1.0 CD2 C:HIS306 3.6 27.2 1.0 CG1 C:ILE257 3.7 32.9 1.0 OD2 A:ASP98 3.8 37.0 1.0 CD2 C:HIS255 3.9 30.0 1.0 CD2 C:LEU308 4.0 28.9 1.0 CE1 C:HIS306 4.0 28.3 1.0 NE2 A:HIS100 4.1 25.3 1.0 NE2 C:HIS255 4.3 33.8 1.0 CG2 C:ILE257 4.4 31.0 1.0 CD2 A:HIS135 4.5 27.9 1.0 CG2 C:VAL304 4.6 24.6 1.0 CB C:ILE257 4.6 30.9 1.0 CG C:HIS306 4.6 31.9 1.0 CD1 C:LEU308 4.8 27.8 1.0 ND1 A:HIS135 4.8 28.2 1.0 ND1 C:HIS306 4.8 26.9 1.0 CD2 A:HIS100 4.9 25.0 1.0 CG A:ASP98 4.9 32.5 1.0 CG C:HIS255 4.9 28.2 1.0 CG C:LEU308 5.0 29.6 1.0

Chlorine binding site 2 out of 3 in the Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:40.8 occ:1.00 CU B:CU402 2.2 34.8 1.0 NE2 A:HIS306 3.1 29.1 1.0 NE2 B:HIS135 3.2 30.5 1.0 CD1 A:ILE257 3.4 32.0 1.0 CE1 B:HIS135 3.5 28.1 1.0 CD2 A:HIS306 3.6 27.0 1.0 CG1 A:ILE257 3.7 35.1 1.0 OD2 B:ASP98 3.8 39.5 1.0 CD2 A:LEU308 3.8 32.2 1.0 CD2 A:HIS255 3.9 27.6 1.0 CE1 A:HIS306 4.0 26.2 1.0 NE2 B:HIS100 4.2 29.4 1.0 NE2 A:HIS255 4.2 29.4 1.0 CG2 A:ILE257 4.4 33.5 1.0 CD2 B:HIS135 4.5 28.8 1.0 CG2 A:VAL304 4.5 34.2 1.0 CB A:ILE257 4.6 31.9 1.0 CG A:HIS306 4.6 28.6 1.0 ND1 A:HIS306 4.8 27.9 1.0 CD1 A:LEU308 4.8 34.8 1.0 ND1 B:HIS135 4.8 28.8 1.0 CG B:ASP98 4.9 33.4 1.0 CG A:HIS255 4.9 28.1 1.0 CG A:LEU308 4.9 33.0 1.0

Chlorine binding site 3 out of 3 in the Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Completely Oxidized Structure of Copper Nitrite Reductase From Alcaligenes Faecalis within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl403 b:35.6 occ:1.00 CU C:CU402 2.2 29.6 1.0 NE2 B:HIS306 3.0 21.3 1.0 NE2 C:HIS135 3.3 25.8 1.0 CE1 C:HIS135 3.4 27.3 1.0 CD1 B:ILE257 3.5 24.0 1.0 CD2 B:HIS306 3.5 24.6 1.0 CG1 B:ILE257 3.6 28.6 1.0 CD2 B:LEU308 3.8 25.3 1.0 OD2 C:ASP98 3.9 33.6 1.0 CE1 B:HIS306 4.0 20.6 1.0 CD2 B:HIS255 4.0 27.6 1.0 NE2 C:HIS100 4.0 22.2 1.0 NE2 B:HIS255 4.3 28.7 1.0 CG2 B:ILE257 4.4 23.4 1.0 CG B:HIS306 4.5 23.5 1.0 CG2 B:VAL304 4.6 23.6 1.0 CB B:ILE257 4.6 25.1 1.0 CD2 C:HIS135 4.6 28.2 1.0 ND1 C:HIS135 4.7 27.1 1.0 ND1 B:HIS306 4.8 23.5 1.0 CD1 B:LEU308 4.8 26.8 1.0 CD2 C:HIS100 4.9 21.4 1.0 CE1 C:HIS100 4.9 22.2 1.0 CG B:HIS255 4.9 25.4 1.0 CG B:LEU308 4.9 25.9 1.0 CG C:ASP98 5.0 30.4 1.0

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.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