Sodium in PDB 7sz9: Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp

All present enzymatic activity of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp:
2.3.1.41;

The structure of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp, PDB code: 7sz9 was solved by J.T.Mindrebo, A.Chen, J.P.Noel, M.D.Burkart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.02 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.45, 103.58, 79.28, 90, 108.28, 90
R / Rfree (%)	20.8 / 25.5

The binding sites of Sodium atom in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp (pdb code 7sz9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp, PDB code: 7sz9:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-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, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Na501 b:34.8 occ:1.00 OE1 A:GLU342 2.4 78.7 1.0 O A:ASN296 2.5 37.1 1.0 OG A:SER387 2.6 39.5 0.6 O A:ASN388 2.7 45.8 1.0 OD1 A:ASN296 2.7 49.5 1.0 O A:SER297 3.1 56.4 1.0 C A:ASN296 3.2 43.9 1.0 N A:ASN388 3.2 37.4 1.0 CD A:GLU342 3.4 77.0 1.0 CG A:ASN296 3.4 42.9 1.0 C A:SER297 3.5 52.3 1.0 CB A:ASN296 3.6 38.3 1.0 C A:ASN388 3.6 42.5 1.0 CB A:SER387 3.7 37.2 0.5 CB A:SER387 3.7 37.2 0.6 CA A:SER387 3.7 41.5 0.5 CA A:SER387 3.8 41.5 0.6 C A:SER387 3.8 39.0 0.5 C A:SER387 3.8 39.0 0.6 N A:SER297 3.9 46.5 1.0 CB A:GLU342 4.0 37.5 1.0 CA A:ASN388 4.0 39.1 1.0 CA A:ASN296 4.0 41.9 1.0 O A:HOH611 4.0 49.9 1.0 N A:HIS298 4.0 53.0 1.0 OE2 A:GLU342 4.0 83.4 1.0 CA A:SER297 4.2 47.2 1.0 CG A:GLU342 4.2 49.2 1.0 CA A:HIS298 4.4 45.1 1.0 ND2 A:ASN296 4.5 46.1 1.0 CB A:ASN388 4.6 37.3 1.0 OG A:SER389 4.7 43.3 1.0 O A:SER387 4.8 33.6 0.5 O A:SER387 4.8 33.7 0.6 N A:SER389 4.9 36.3 1.0 OG A:SER387 4.9 37.6 0.5

Sodium binding site 2 out of 2 in the Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-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 2 of Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, Fabb, and C16:1-Crypto Acyl Carrier Protein, Acpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Na501 b:39.5 occ:1.00 OE1 B:GLU342 2.3 58.5 1.0 O B:ASN296 2.4 37.4 1.0 O B:ASN388 2.5 32.5 1.0 OD1 B:ASN296 2.7 34.9 1.0 OG B:SER387 2.7 25.8 0.7 O B:SER297 3.1 48.9 1.0 N B:ASN388 3.1 33.8 1.0 C B:ASN296 3.3 43.9 1.0 C B:SER297 3.4 39.8 1.0 C B:ASN388 3.5 37.1 1.0 CD B:GLU342 3.5 70.2 1.0 CG B:ASN296 3.6 38.4 1.0 CB B:SER387 3.7 30.2 0.3 CB B:SER387 3.7 29.8 0.7 C B:SER387 3.8 34.0 0.3 C B:SER387 3.8 34.2 0.7 CA B:SER387 3.8 35.8 0.3 CA B:SER387 3.8 34.4 0.7 CA B:ASN388 3.9 35.6 1.0 N B:HIS298 3.9 49.1 1.0 CB B:ASN296 3.9 28.7 1.0 N B:SER297 4.1 38.0 1.0 CA B:HIS298 4.1 49.0 1.0 CA B:SER297 4.1 44.6 1.0 CB B:GLU342 4.2 32.4 1.0 CA B:ASN296 4.2 29.3 1.0 OE2 B:GLU342 4.3 64.3 1.0 CG B:GLU342 4.4 35.1 1.0 CB B:ASN388 4.6 32.6 1.0 OG B:SER389 4.6 33.2 1.0 N B:SER389 4.7 34.5 1.0 O B:SER387 4.7 30.6 0.3 O B:SER387 4.8 32.1 0.7 OG B:SER387 4.8 33.8 0.3 ND2 B:ASN296 4.9 35.6 1.0 CB B:HIS298 5.0 40.5 1.0

A.Chen, J.T.Mindrebo, T.D.Davis, W.E.Kim, Y.Katsuyama, Z.Jiang, Y.Ohnishi, J.P.Noel, M.D.Burkart. Mechanism-Based Cross-Linking Probes Capture the Escherichia Coli Ketosynthase Fabb in Conformationally Distinct Catalytic States. Acta Crystallogr D Struct V. 78 1171 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 36048156
DOI: 10.1107/S2059798322007434