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Sodium in PDB 2fad: Crystal Structure of E. Coli Heptanoyl-Acp

Protein crystallography data

The structure of Crystal Structure of E. Coli Heptanoyl-Acp, PDB code: 2fad was solved by A.Roujeinikova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.60
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 49.257, 106.244, 28.195, 90.00, 90.00, 90.00
R / Rfree (%) 20.9 / 25.6

Other elements in 2fad:

The structure of Crystal Structure of E. Coli Heptanoyl-Acp also contains other interesting chemical elements:

Zinc (Zn) 8 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of E. Coli Heptanoyl-Acp (pdb code 2fad). 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 Crystal Structure of E. Coli Heptanoyl-Acp, PDB code: 2fad:

Sodium binding site 1 out of 1 in 2fad

Go back to Sodium Binding Sites List in 2fad
Sodium binding site 1 out of 1 in the Crystal Structure of E. Coli Heptanoyl-Acp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of E. Coli Heptanoyl-Acp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na401

b:8.6
occ:1.00
OD1 B:ASP51 2.0 22.5 1.0
O B:HOH472 2.1 36.7 1.0
N A:SER1 2.5 17.2 1.0
O A:SER1 2.7 23.9 1.0
CG B:ASP51 2.7 20.2 1.0
OD2 B:ASP51 2.9 25.6 1.0
C A:SER1 3.3 25.0 1.0
CA A:SER1 3.4 16.5 1.0
O B:HOH444 3.8 36.3 1.0
O B:HOH439 3.9 1.2 0.5
O B:HOH443 4.0 34.9 1.0
O B:HOH410 4.2 20.3 1.0
O B:HOH442 4.2 21.1 0.5
CB B:ASP51 4.2 29.9 1.0
O B:GLU49 4.2 18.4 1.0
N A:THR2 4.4 15.0 1.0
CB A:SER1 4.7 17.6 1.0
OG A:SER1 4.7 21.1 1.0
O A:HOH472 4.7 31.1 1.0
O B:HOH424 4.8 22.2 1.0
N B:ASP51 4.8 18.8 1.0

Reference:

A.Roujeinikova, W.J.Simon, J.Gilroy, D.W.Rice, J.B.Rafferty, A.R.Slabas. Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal A Hydrophobic Binding Cavity That Can Expand to Fit Longer Substrates. J.Mol.Biol. V. 365 135 2007.
ISSN: ISSN 0022-2836
PubMed: 17059829
DOI: 10.1016/J.JMB.2006.09.049
Page generated: Tue Dec 15 05:48:54 2020

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