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Sodium in PDB 3zu4: Structure of the Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172

Protein crystallography data

The structure of Structure of the Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172, PDB code: 3zu4 was solved by M.W.Hirschbeck, J.Kuper, P.J.Tonge, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 88.20 / 2.01
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 101.840, 101.840, 84.750, 90.00, 90.00, 120.00
R / Rfree (%) 17.6 / 22.1

Other elements in 3zu4:

The structure of Structure of the Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172 also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of the Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172 (pdb code 3zu4). 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 Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172, PDB code: 3zu4:

Sodium binding site 1 out of 1 in 3zu4

Go back to Sodium Binding Sites List in 3zu4
Sodium binding site 1 out of 1 in the Structure of the Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172


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 Enoyl-Acp Reductase Fabv From Yersinia Pestis with the Cofactor Nadh and the 2-Pyridone Inhibitor PT172 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1402

b:40.1
occ:1.00
N A:GLY54 2.8 24.8 1.0
OG A:SER138 2.9 28.3 0.8
O A:THR51 2.9 24.1 1.0
O5B A:NAI1400 3.0 32.8 1.0
O2N A:NAI1400 3.2 32.9 1.0
O A:SER138 3.3 30.0 1.0
O A:GLY48 3.3 27.3 1.0
C5D A:NAI1400 3.5 32.7 1.0
CA A:GLY54 3.5 25.9 1.0
N A:TYR53 3.6 25.0 1.0
C5B A:NAI1400 3.7 29.3 1.0
C4B A:NAI1400 3.7 29.1 1.0
OG A:SER138 3.9 28.9 0.2
O3 A:NAI1400 3.9 31.9 1.0
PN A:NAI1400 3.9 34.0 1.0
C A:TYR53 3.9 24.9 1.0
CB A:SER138 3.9 29.3 0.2
CB A:SER138 3.9 29.0 0.8
PA A:NAI1400 4.0 31.9 1.0
C A:THR51 4.0 23.5 1.0
O5D A:NAI1400 4.0 34.8 1.0
O1A A:NAI1400 4.1 35.1 1.0
C A:GLY52 4.1 25.6 1.0
CA A:TYR53 4.1 25.6 1.0
C A:SER138 4.3 30.5 1.0
C A:GLY48 4.4 25.9 1.0
CA A:GLY52 4.4 24.9 1.0
N A:LEU55 4.4 26.0 1.0
CB A:TYR53 4.5 24.9 1.0
C A:GLY54 4.5 26.2 1.0
C3B A:NAI1400 4.5 28.9 1.0
N A:GLY52 4.7 24.4 1.0
O3B A:NAI1400 4.7 27.5 1.0
OG1 A:THR51 4.7 24.0 1.0
CA A:SER138 4.7 30.2 0.8
CA A:SER138 4.7 30.1 0.2
O A:GLY52 4.8 25.5 1.0
C4D A:NAI1400 4.8 32.0 1.0
O4B A:NAI1400 4.9 31.3 1.0
CA A:GLY48 4.9 26.7 1.0

Reference:

M.W.Hirschbeck, J.Kuper, H.Lu, N.Liu, C.Neckles, S.Shah, S.Wagner, C.A.Sotriffer, P.J.Tonge, C.Kisker. Structure of the Yersinia Pestis Fabv Enoyl-Acp Reductase and Its Interaction with Two 2-Pyridone Inhibitors Structure V. 20 89 2012.
ISSN: ISSN 0969-2126
PubMed: 22244758
DOI: 10.1016/J.STR.2011.07.019
Page generated: Tue Dec 15 06:32:00 2020

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