Zinc in PDB 7oso: The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol

All present enzymatic activity of The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol:
2.4.1.10;

The structure of The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol, PDB code: 7oso was solved by I.Polsinelli, M.Salomone-Stagni, S.Benini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.19 / 1.40
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	127.713, 127.713, 61.016, 90, 90, 90
R / Rfree (%)	13.3 / 16.4

The binding sites of Zinc atom in the The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol (pdb code 7oso). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol, PDB code: 7oso:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:25.4 occ:1.00 OE2 A:GLU141 1.9 25.7 1.0 OD1 A:ASP140 2.0 22.8 1.0 O A:HOH974 2.2 17.5 1.0 CD A:GLU141 2.7 25.3 1.0 OE1 A:GLU141 2.9 25.3 1.0 CG A:ASP140 3.1 23.3 1.0 OD2 A:ASP140 3.5 26.5 1.0 O A:HOH729 4.1 31.7 1.0 CG A:GLU141 4.2 24.7 1.0 N A:ASP140 4.3 21.4 1.0 CG A:LYS415 4.3 38.1 1.0 CB A:ASP140 4.4 23.0 1.0 N A:GLU141 4.4 21.9 1.0 C A:ASP140 4.5 22.5 1.0 CA A:ASP140 4.6 21.1 1.0 O A:HOH953 4.6 22.4 1.0 CB A:ASN139 4.9 22.2 1.0 O A:ASP140 5.0 26.2 1.0

Zinc binding site 2 out of 3 in the The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn502 b:30.1 occ:1.00 OD2 A:ASP56 1.9 28.9 1.0 OD2 A:ASP52 2.0 26.1 1.0 OD2 A:ASP54 2.1 29.5 1.0 O A:HOH942 2.2 24.7 1.0 CG A:ASP52 2.8 23.0 1.0 CG A:ASP54 2.9 30.7 1.0 CG A:ASP56 2.9 33.3 1.0 OD1 A:ASP52 3.0 21.4 1.0 OD1 A:ASP54 3.2 28.3 1.0 CB A:ASP56 3.4 29.9 1.0 O A:HOH640 3.8 42.7 1.0 O A:HOH949 3.8 38.0 1.0 NZ A:LYS410 4.0 36.0 1.0 OD1 A:ASP56 4.0 37.7 1.0 CB A:ASP52 4.2 20.8 1.0 CB A:ASP54 4.3 24.7 1.0 CD A:LYS410 4.4 42.6 1.0 CA A:ASP56 4.6 26.5 1.0 CE A:LYS410 4.7 41.5 1.0 N A:ASP56 4.7 28.2 1.0 N A:ASP54 4.9 28.8 1.0

Zinc binding site 3 out of 3 in the The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn503 b:28.7 occ:1.00 O A:HOH912 1.9 32.0 1.0 OD2 A:ASP317 2.0 24.8 1.0 ND1 A:HIS305 2.1 23.6 1.0 O A:HOH978 2.2 19.3 1.0 OD1 A:ASP317 2.6 24.7 1.0 CG A:ASP317 2.6 22.1 1.0 CE1 A:HIS305 3.1 26.8 1.0 CG A:HIS305 3.2 22.3 1.0 CB A:HIS305 3.5 21.9 1.0 CA A:HIS305 3.9 20.0 1.0 CE1 A:PHE349 4.0 43.9 1.0 O A:HOH607 4.0 38.6 1.0 CB A:ASP317 4.1 20.6 1.0 CD1 A:PHE349 4.1 38.5 1.0 NE2 A:HIS305 4.2 27.3 1.0 CD2 A:HIS305 4.3 24.1 1.0 O A:HOH718 4.3 25.0 1.0 N A:LYS306 4.4 20.4 1.0 CE1 A:TYR352 4.6 23.0 1.0 C A:HIS305 4.7 19.9 1.0 CD1 A:TYR352 4.7 21.1 1.0 CA A:ASP317 5.0 20.2 1.0

I.Polsinelli, M.Salomone-Stagni, S.Benini. The Crystal Structure of Erwinia Tasmaniensis Levansucrase in Complex with (S)-1,2,4-Butanentriol Reveals Enzymatic Enantiomer Selection and Hints at Different Fructose Binding Modes in Gram+ and Gram-. To Be Published.