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Sodium in PDB 3uu9: Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase

Protein crystallography data

The structure of Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase, PDB code: 3uu9 was solved by A.A.Trofimov, K.M.Polyakov, T.V.Tikhonova, A.V.Tikhonov, P.V.Dorovatovskii, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 2.20
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 191.387, 191.387, 191.387, 90.00, 90.00, 90.00
R / Rfree (%) 15.7 / 18.4

Other elements in 3uu9:

The structure of Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase also contains other interesting chemical elements:

Iron (Fe) 16 atoms
Calcium (Ca) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase (pdb code 3uu9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase, PDB code: 3uu9:

Sodium binding site 1 out of 1 in 3uu9

Go back to Sodium Binding Sites List in 3uu9
Sodium binding site 1 out of 1 in the Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of the Free Tvnirb Form of Thioalkalivibrio Nitratireducens Cytochrome C Nitrite Reductase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na621

b:36.7
occ:1.00
O1A B:HEC604 2.4 30.5 0.5
O1A B:HEC604 2.7 28.8 0.5
N B:THR402 2.7 28.0 1.0
O2A B:HEC603 2.8 26.9 1.0
CGA B:HEC603 3.2 28.6 1.0
CGA B:HEC604 3.4 32.0 0.5
CA B:ARG401 3.4 28.6 1.0
C B:ARG401 3.5 28.2 1.0
OG B:SER84 3.6 29.7 1.0
CB B:THR402 3.7 28.3 1.0
CG2 B:THR402 3.7 29.6 1.0
CA B:THR402 3.7 28.2 1.0
CB B:ARG401 3.7 28.3 1.0
CGA B:HEC604 3.7 29.1 0.5
CD B:ARG81 3.8 27.2 1.0
O1A B:HEC603 3.8 25.5 1.0
O B:HOH729 3.8 30.5 1.0
CBA B:HEC603 3.8 23.7 1.0
CBA B:HEC604 4.0 27.7 1.0
NH1 B:ARG81 4.1 27.5 1.0
NE B:ARG81 4.2 27.6 1.0
O2A B:HEC604 4.2 32.0 0.5
CAA B:HEC603 4.2 24.0 1.0
CMA B:HEC603 4.3 25.4 1.0
CZ B:ARG81 4.4 28.3 1.0
O B:HOH746 4.6 29.9 1.0
O B:ARG401 4.7 28.8 1.0
N B:ARG401 4.8 29.6 1.0
O2A B:HEC604 4.8 27.9 0.5
O B:GLN400 4.9 30.4 1.0
CA B:CA610 4.9 42.3 0.5
CB B:SER84 5.0 29.4 1.0
CG B:ARG401 5.0 29.6 1.0

Reference:

A.A.Trofimov, K.M.Polyakov, T.V.Tikhonova, A.V.Tikhonov, T.N.Safonova, K.M.Boyko, P.V.Dorovatovskii, V.O.Popov. Covalent Modifications of the Catalytic Tyrosine in Octahaem Cytochrome C Nitrite Reductase and Their Effect on the Enzyme Activity. Acta Crystallogr.,Sect.D V. 68 144 2012.
ISSN: ISSN 0907-4449
PubMed: 22281743
DOI: 10.1107/S0907444911052632
Page generated: Mon Oct 7 13:34:57 2024

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