Magnesium in PDB 4dn1: Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate

The structure of Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate, PDB code: 4dn1 was solved by M.W.Vetting, R.Toro, R.Bhosle, J.T.Bouvier, S.R.Wasserman, L.L.Morisco, S.Sojitra, N.F.Al Obaidi, H.J.Imker, J.A.Gerlt, S.C.Almo, Enzyme Functioninitiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.71 / 2.05
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.360, 102.360, 369.620, 90.00, 90.00, 120.00
R / Rfree (%)	16.1 / 19.4

The structure of Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate (pdb code 4dn1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate, PDB code: 4dn1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate


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 An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:16.6 occ:1.00 OE2 A:GLU240 2.0 23.1 1.0 O A:HOH763 2.1 29.8 1.0 OE1 A:GLU266 2.1 24.6 1.0 O A:HOH713 2.1 22.3 1.0 O2 A:FMT402 2.2 27.9 1.0 OD2 A:ASP214 2.2 26.0 1.0 C A:FMT402 2.9 31.7 1.0 CD A:GLU266 2.9 25.2 1.0 OE2 A:GLU266 3.1 28.1 1.0 CD A:GLU240 3.1 29.9 1.0 CG A:ASP214 3.2 24.3 1.0 OD1 A:ASP214 3.5 21.1 1.0 CG A:GLU240 4.0 23.1 1.0 OE1 A:GLU240 4.0 26.5 1.0 O A:HOH560 4.0 25.5 1.0 NZ A:LYS184 4.0 25.0 1.0 O1 A:FMT402 4.1 31.6 1.0 O A:HOH538 4.3 19.9 1.0 CG A:GLU266 4.3 16.7 1.0 CH2 A:TRP217 4.4 27.3 1.0 CD2 A:HIS315 4.4 24.6 1.0 CB A:ASP214 4.5 27.0 1.0 O A:HOH628 4.6 31.9 1.0 NE2 A:HIS315 4.7 22.6 1.0 O A:HOH663 4.8 34.7 1.0 CZ2 A:TRP217 4.8 27.3 1.0 CE A:LYS184 5.0 25.1 1.0 NE2 A:HIS216 5.0 36.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:9.7 occ:1.00 OE2 B:GLU240 2.0 26.4 1.0 O B:HOH788 2.1 24.8 1.0 O B:HOH510 2.1 17.8 1.0 O B:HOH786 2.1 25.5 1.0 OE1 B:GLU266 2.2 19.6 1.0 OD2 B:ASP214 2.2 17.7 1.0 CD B:GLU266 3.2 23.1 1.0 CD B:GLU240 3.2 26.0 1.0 CG B:ASP214 3.3 25.7 1.0 OE2 B:GLU266 3.4 28.2 1.0 OD1 B:ASP214 3.6 20.7 1.0 OE1 B:GLU240 4.0 25.6 1.0 O B:HOH539 4.1 22.7 1.0 CG B:GLU240 4.2 19.7 1.0 NZ B:LYS184 4.3 22.0 1.0 O B:HOH784 4.3 22.4 1.0 CD2 B:HIS315 4.4 14.2 1.0 O B:HOH513 4.5 20.9 1.0 OE2 B:GLU341 4.5 33.2 1.0 CB B:ASP214 4.5 19.8 1.0 CG B:GLU266 4.6 14.4 1.0 CH2 B:TRP217 4.6 17.6 1.0 O B:HOH668 4.7 39.6 1.0 NE2 B:HIS315 4.7 15.5 1.0 CE B:LYS184 4.9 18.4 1.0 NE2 B:HIS216 5.0 29.6 1.0 CZ2 B:TRP217 5.0 17.1 1.0

M.W.Vetting, R.Toro, R.Bhosle, J.T.Bouvier, S.R.Wasserman, L.L.Morisco, S.Sojitra, N.F.Al Obaidi, H.J.Imker, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi). Crystal Structure of An Enolase (Mandelate Racemase Subgroup Member) From Agrobacterium Tumefaciens (Target Efi-502088) with Bound Mg and Formate To Be Published.