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Sodium in PDB 6okg: Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp

Enzymatic activity of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp

All present enzymatic activity of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp:
2.3.1.179;

Protein crystallography data

The structure of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp, PDB code: 6okg was solved by J.T.Mindrebo, W.E.Kim, T.G.Bartholow, A.Chen, T.D.Davis, J.La Clair, M.D.Burkart, J.P.Noel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.05 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 86.890, 86.890, 113.729, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.8

Sodium Binding Sites:

The binding sites of Sodium atom in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp (pdb code 6okg). 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 Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp, PDB code: 6okg:

Sodium binding site 1 out of 1 in 6okg

Go back to Sodium Binding Sites List in 6okg
Sodium binding site 1 out of 1 in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabf, and C16-Crypto Acyl Carrier Protein, Acpp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na501

b:23.8
occ:1.00
 OE1 A:GLU349 2.5 24.6 1.0
O A:ASN301 2.5 25.0 1.0
OD1 A:ASN301 2.5 26.0 1.0
O A:ASN396 2.6 23.6 1.0
O A:ALA302 2.8 22.3 1.0
C A:ASN301 3.3 25.6 1.0
C A:ALA302 3.3 23.5 1.0
CD A:GLU349 3.4 23.9 1.0
N A:ASN396 3.5 25.5 1.0
CG A:ASN301 3.5 25.3 1.0
C A:ASN396 3.6 23.6 1.0
CB A:GLU349 3.7 19.9 1.0
SG A:CYS395 3.8 30.3 1.0
CB A:ASN301 3.9 24.3 1.0
N A:HIS303 3.9 23.1 1.0
O A:HOH633 4.0 19.6 1.0
CG A:GLU349 4.0 22.1 1.0
N A:ALA302 4.0 25.5 1.0
CA A:ASN396 4.1 24.9 1.0
O A:HOH674 4.1 30.6 1.0
CA A:ALA302 4.1 24.4 1.0
CA A:ASN301 4.2 24.7 1.0
CA A:HIS303 4.2 23.7 1.0
OE2 A:GLU349 4.3 24.1 1.0
C A:CYS395 4.4 25.3 1.0
CA A:CYS395 4.5 25.7 1.0
CB A:ASN396 4.6 25.8 1.0
ND2 A:ASN301 4.7 25.1 1.0
N A:SER397 4.8 23.2 1.0
NZ A:LYS335 4.8 18.7 1.0
CB A:CYS395 4.9 27.6 1.0

Reference:

J.T.Mindrebo, A.Patel, W.E.Kim, T.D.Davis, A.Chen, T.G.Bartholow, J.J.La Clair, J.A.Mccammon, J.P.Noel, M.D.Burkart. Gating Mechanism of Elongating Beta-Ketoacyl-Acp Synthases. Nat Commun V. 11 1727 2020.
ISSN: ESSN 2041-1723
PubMed: 32265440
DOI: 10.1038/S41467-020-15455-X
Page generated: Tue Oct 8 12:31:24 2024

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