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Magnesium in PDB 3va8: Crystal Structure of Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate

Protein crystallography data

The structure of Crystal Structure of Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate, PDB code: 3va8 was solved by Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo, Enzyme Function Initiative (Efi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 135.669, 135.669, 164.246, 90.00, 90.00, 120.00
R / Rfree (%) 17 / 21.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate (pdb code 3va8). 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 Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate, PDB code: 3va8:

Magnesium binding site 1 out of 1 in 3va8

Go back to Magnesium Binding Sites List in 3va8
Magnesium binding site 1 out of 1 in the Crystal Structure of Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate


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 Enolase FG03645.1 (Target Efi-502278) From Gibberella Zeae pH-1 Complexed with Magnesium, Formate and Sulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg425

b:40.0
occ:1.00
OE2 A:GLU245 1.8 44.7 1.0
O A:HOH428 2.0 37.3 1.0
OD2 A:ASP220 2.0 35.4 1.0
OD1 A:ASN268 2.0 43.0 1.0
O1 A:FMT426 2.2 42.3 1.0
O2 A:FMT426 2.3 38.0 1.0
C A:FMT426 2.5 49.1 1.0
CG A:ASP220 2.9 33.8 1.0
CD A:GLU245 2.9 43.0 1.0
CG A:ASN268 3.0 38.6 1.0
OD1 A:ASP220 3.3 35.2 1.0
ND2 A:ASN268 3.4 39.8 1.0
CG A:GLU245 3.6 36.4 1.0
NZ A:LYS190 3.7 48.1 1.0
ND2 A:ASN222 3.9 36.4 1.0
OE1 A:GLU245 3.9 49.3 1.0
OD2 A:ASP246 4.1 36.0 1.0
CB A:ASP220 4.1 32.2 1.0
NZ A:LYS192 4.2 43.6 1.0
CB A:ASN268 4.4 34.9 1.0
CD2 A:HIS319 4.5 45.9 1.0
CE A:LYS190 4.6 59.5 1.0
CD1 A:LEU290 4.7 43.2 1.0
CG A:ASN222 4.8 35.1 1.0
OH A:TYR148 4.8 46.8 1.0
N A:ASN268 4.8 30.5 1.0
CB A:GLU245 4.9 32.7 1.0
O A:HOH548 4.9 47.3 1.0
OD1 A:ASN222 5.0 37.3 1.0

Reference:

Y.Patskovsky, R.Toro, R.Bhosle, B.Hillerich, R.D.Seidel, E.Washington, A.Scott Glenn, S.Chowdhury, B.Evans, J.Hammonds, W.D.Zencheck, H.J.Imker, J.A.Gerlt, S.C.Almo. Crystal Structure of Dehydratase FG03645.1 From Gibberella Zeae pH-1 To Be Published.
Page generated: Thu Aug 15 12:51:10 2024

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