Sodium in PDB 3lrf: Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis

All present enzymatic activity of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis:
2.3.1.41;

The structure of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis, PDB code: 3lrf was solved by J.Abendroth, T.Edwards, B.Staker, Seattle Structural Genomics Center Forinfectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.480, 83.270, 72.870, 90.00, 120.97, 90.00
R / Rfree (%)	12.9 / 15.8

The binding sites of Sodium atom in the Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis (pdb code 3lrf). 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 Beta-Ketoacyl Synthase From Brucella Melitensis, PDB code: 3lrf:

Sodium binding site 1 out of 1 in the Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis


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 Beta-Ketoacyl Synthase From Brucella Melitensis within 5.0Å range: probe atom residue distance (Å) B Occ A:Na500 b:8.8 occ:1.00 OD1 A:ASN294 2.3 6.4 1.0 OE1 A:GLU342 2.3 8.5 1.0 O A:ASN389 2.5 7.7 1.0 O A:ASN294 2.5 7.0 1.0 OG A:SER388 2.5 8.3 1.0 O A:PRO295 2.7 8.4 1.0 O A:HOH894 2.8 30.5 1.0 CD A:GLU342 3.3 9.1 1.0 C A:ASN294 3.3 7.1 1.0 C A:PRO295 3.4 8.6 1.0 CG A:ASN294 3.4 6.5 1.0 N A:ASN389 3.4 6.5 1.0 C A:ASN389 3.5 7.5 1.0 CB A:SER388 3.7 7.5 1.0 CB A:ASN294 3.8 7.4 1.0 CB A:GLU342 3.9 6.2 1.0 C A:SER388 3.9 6.9 1.0 CA A:SER388 3.9 7.2 1.0 N A:PRO295 4.0 6.8 1.0 CA A:ASN389 4.0 6.8 1.0 N A:HIS296 4.0 8.4 1.0 OE2 A:GLU342 4.1 13.5 1.0 O A:HOH531 4.1 10.5 1.0 CG A:GLU342 4.1 6.6 1.0 CA A:PRO295 4.1 8.1 1.0 CA A:ASN294 4.2 7.4 1.0 CA A:HIS296 4.4 9.7 1.0 O A:HOH520 4.5 10.1 1.0 ND2 A:ASN294 4.6 8.9 1.0 OG A:SER390 4.6 17.8 1.0 N A:SER390 4.7 9.2 1.0 CB A:ASN389 4.7 7.3 1.0 NZ A:LYS328 4.7 10.0 1.0 O A:SER388 4.8 7.4 1.0

E.I.Patterson, J.D.Nanson, J.Abendroth, C.Bryan, B.Sankaran, P.J.Myler, J.K.Forwood. Structural Characterization of Beta-Ketoacyl Acp Synthase I Bound to Platencin and Fragment Screening Molecules at Two Substrate Binding Sites. Proteins 2019.
ISSN: ESSN 1097-0134
PubMed: 31237717
DOI: 10.1002/PROT.25765