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Sodium in PDB 1jju: Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking

Protein crystallography data

The structure of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking, PDB code: 1jju was solved by S.Datta, Y.Mori, K.Takagi, K.Kawaguchi, Z.-W.Chen, K.Kano, T.Ikeda, T.Okajima, S.Kuroda, K.Tanizawa, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.05
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 99.489, 99.489, 214.489, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 25.1

Other elements in 1jju:

The structure of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking (pdb code 1jju). 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 A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking, PDB code: 1jju:

Sodium binding site 1 out of 1 in 1jju

Go back to Sodium Binding Sites List in 1jju
Sodium binding site 1 out of 1 in the Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of A Quinohemoprotein Amine Dehydrogenase with A Unique Redox Cofactor and Highly Unusual Crosslinking within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Na996

b:51.3
occ:1.00
OD1 C:ASP33 2.1 29.5 1.0
O C:TBU993 2.4 54.8 1.0
O6 C:TRQ43 2.4 27.9 1.0
OD2 C:ASP33 2.5 30.8 1.0
CG C:ASP33 2.6 30.4 1.0
O B:HOH1167 2.7 40.3 1.0
CZ B:PHE244 3.4 29.0 1.0
C C:TBU993 3.5 48.2 1.0
C1 C:TBU993 3.5 43.3 1.0
CH2 C:TRQ43 3.5 30.9 1.0
O C:ASP12 3.7 30.8 1.0
CD C:PRO13 3.9 28.3 1.0
CZ3 C:TRQ43 4.0 28.4 1.0
OH B:TYR283 4.0 25.5 1.0
CB C:ASP33 4.0 27.3 1.0
CE1 B:PHE244 4.1 32.0 1.0
C2 C:TBU993 4.1 48.4 1.0
CE2 B:PHE244 4.3 34.7 1.0
SG C:CYS27 4.3 28.6 1.0
C C:ASP12 4.6 32.4 1.0
O C:ASP33 4.6 27.4 1.0
O C:HOH1031 4.6 36.4 1.0
CE2 B:TYR283 4.7 30.4 1.0
CZ B:TYR283 4.7 29.4 1.0
CZ2 C:TRQ43 4.7 30.9 1.0
C3 C:TBU993 4.7 49.1 1.0
N C:PRO13 4.7 32.5 1.0
CA C:ASP33 4.9 27.9 1.0
O7 C:TRQ43 4.9 29.0 1.0
CG C:PRO13 5.0 35.0 1.0

Reference:

S.Datta, Y.Mori, K.Takagi, K.Kawaguchi, Z.W.Chen, T.Okajima, S.Kuroda, T.Ikeda, K.Kano, K.Tanizawa, F.S.Mathews. Structure of A Quinohemoprotein Amine Dehydrogenase with An Uncommon Redox Cofactor and Highly Unusual Crosslinking. Proc.Natl.Acad.Sci.Usa V. 98 14268 2001.
ISSN: ISSN 0027-8424
PubMed: 11717396
DOI: 10.1073/PNAS.241429098
Page generated: Tue Dec 15 05:26:11 2020

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