Zinc in PDB 5fgn: Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis

The structure of Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis, PDB code: 5fgn was solved by A.Anandan, A.Vrielink, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.82 / 2.75
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	187.285, 187.285, 205.125, 90.00, 90.00, 90.00
R / Rfree (%)	21.4 / 24.1

The binding sites of Zinc atom in the Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis (pdb code 5fgn). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis, PDB code: 5fgn:

Zinc binding site 1 out of 1 in the Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Integral Membrane Protein Lipooligosaccharide Phosphoethanolamine Transferase A (Epta) From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn603 b:44.8 occ:1.00 OE2 A:GLU240 1.6 46.6 1.0 OD2 A:ASP452 1.8 40.8 1.0 OG1 A:THR280 1.8 41.8 1.0 NE2 A:HIS453 1.9 41.0 1.0 CD A:GLU240 2.4 45.0 1.0 OE1 A:GLU240 2.6 55.5 1.0 CD2 A:HIS453 2.7 40.9 1.0 CG A:ASP452 2.8 57.6 1.0 CE1 A:HIS453 3.0 41.8 1.0 CB A:THR280 3.1 42.2 1.0 OD1 A:ASP452 3.3 52.3 1.0 CA A:THR280 3.4 42.2 1.0 N A:THR280 3.5 42.2 1.0 O3B A:LMT602 3.7 42.4 1.0 CG A:GLU240 3.8 42.0 1.0 CG2 A:THR280 3.8 42.2 1.0 CG A:HIS453 3.8 40.7 1.0 ND1 A:HIS453 3.9 40.6 1.0 CB A:ASP452 4.1 40.5 1.0 O A:HOH760 4.2 57.5 1.0 C A:SER279 4.3 42.2 1.0 OG1 A:THR241 4.4 40.5 1.0 N A:THR241 4.4 39.7 1.0 NE2 A:HIS465 4.5 41.9 1.0 CA A:GLU240 4.6 39.8 1.0 CB A:GLU240 4.6 40.2 1.0 CE1 A:HIS465 4.8 41.6 1.0 CA A:SER279 4.9 42.2 1.0 O A:SER279 4.9 42.2 1.0 C A:THR280 4.9 42.7 1.0 C A:GLU240 5.0 39.6 1.0

A.Anandan, G.L.Evans, K.Condic-Jurkic, M.L.O'mara, C.M.John, N.J.Phillips, G.A.Jarvis, S.S.Wills, K.A.Stubbs, I.Moraes, C.M.Kahler, A.Vrielink. Structure of A Lipid A Phosphoethanolamine Transferase Suggests How Conformational Changes Govern Substrate Binding. Proc. Natl. Acad. Sci. V. 114 2218 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28193899
DOI: 10.1073/PNAS.1612927114