Magnesium in PDB 2hxt: Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate

The structure of Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate, PDB code: 2hxt was solved by A.A.Fedorov, E.V.Fedorov, W.S.Yew, J.F.Rakus, J.A.Gerlt, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.80 / 1.70
Space group	P 6 2 2
Cell size a, b, c (Å), α, β, γ (°)	159.533, 159.533, 102.069, 90.00, 90.00, 120.00
R / Rfree (%)	17.9 / 19.7

The binding sites of Magnesium atom in the Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate (pdb code 2hxt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate, PDB code: 2hxt:

Magnesium binding site 1 out of 1 in the Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of L-Fuconate Dehydratase From Xanthomonas Campestris Liganded with Mg++ and D-Erythronohydroxamate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:15.7 occ:1.00 OE1 A:GLU301 2.2 12.6 1.0 OD2 A:ASP248 2.3 11.3 1.0 O A:HOH648 2.3 12.3 1.0 OE2 A:GLU274 2.3 13.6 1.0 O1 A:EHM501 2.4 13.7 1.0 ON A:EHM501 2.5 15.8 1.0 CD A:GLU301 3.2 12.1 1.0 C1 A:EHM501 3.2 15.1 1.0 CD A:GLU274 3.2 12.7 1.0 CG A:ASP248 3.2 12.0 1.0 N A:EHM501 3.3 14.4 1.0 OE2 A:GLU301 3.5 12.7 1.0 OD1 A:ASP248 3.5 10.6 1.0 NZ A:LYS218 3.7 12.9 1.0 NZ A:LYS220 3.7 12.6 1.0 CG A:GLU274 3.9 9.2 1.0 O A:HOH632 3.9 12.4 1.0 OE1 A:GLU274 4.1 12.0 1.0 OD1 A:ASN250 4.2 14.8 1.0 CD2 A:HIS351 4.2 10.8 1.0 O A:HOH603 4.3 10.5 1.0 CG A:GLU301 4.4 10.0 1.0 OE2 A:GLU275 4.5 11.7 1.0 CB A:ASP248 4.6 9.6 1.0 C2 A:EHM501 4.6 15.0 1.0 CE A:LYS218 4.7 16.1 1.0 CB A:GLU274 4.8 8.9 1.0 CG A:ASN250 4.8 12.4 1.0 NE2 A:HIS351 4.8 11.8 1.0 ND2 A:ASN250 4.9 11.8 1.0

W.S.Yew, A.A.Fedorov, E.V.Fedorov, J.F.Rakus, R.W.Pierce, S.C.Almo, J.A.Gerlt. Evolution of Enzymatic Activities in the Enolase Superfamily: L-Fuconate Dehydratase From Xanthomonas Campestris. Biochemistry V. 45 14582 2006.
ISSN: ISSN 0006-2960
PubMed: 17144652
DOI: 10.1021/BI061687O