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Magnesium in PDB 3r10: Crystal Structure of Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex

Protein crystallography data

The structure of Crystal Structure of Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex, PDB code: 3r10 was solved by M.W.Vetting, B.Hillerich, R.D.Seidel, W.D.Zencheck, R.Toro, H.J.Imker, J.A.Gerlt, S.C.Almo, New York Structural Genomics Research Consortium(Nysgrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.34 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 120.680, 120.680, 150.020, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 19.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex (pdb code 3r10). 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 Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex, PDB code: 3r10:

Magnesium binding site 1 out of 1 in 3r10

Go back to Magnesium Binding Sites List in 3r10
Magnesium binding site 1 out of 1 in the Crystal Structure of Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex


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 Nysgrc Enolase Target 200555, A Putative Dipeptide Epimerase From Francisella Philomiragia : Mg Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg384

b:15.8
occ:1.00
OE2 A:GLU220 2.2 14.1 1.0
O A:HOH549 2.2 10.0 1.0
O A:HOH550 2.2 11.3 1.0
OD2 A:ASP245 2.2 10.5 1.0
OD2 A:ASP192 2.2 13.3 1.0
O A:HOH548 2.2 10.4 1.0
CD A:GLU220 3.1 17.3 1.0
CG A:ASP192 3.1 15.3 1.0
CG A:ASP245 3.2 14.3 1.0
OD1 A:ASP192 3.4 13.5 1.0
CB A:ASP245 3.6 9.2 1.0
CG A:GLU220 3.8 13.1 1.0
O A:HOH543 3.9 21.7 1.0
OE1 A:GLU220 3.9 16.1 1.0
NZ A:LYS269 4.0 12.2 1.0
OE1 A:GLU246 4.1 14.9 1.0
OE2 A:GLU246 4.1 17.9 1.0
ND2 A:ASN267 4.1 8.7 1.0
O A:HOH556 4.2 29.0 1.0
O A:HOH591 4.2 40.3 1.0
OD1 A:ASP245 4.4 10.8 1.0
CB A:ASP192 4.4 13.8 1.0
CD A:GLU246 4.5 16.3 1.0
CE A:LYS269 4.6 8.9 1.0
O A:HOH410 4.8 12.1 1.0
CB A:GLU220 5.0 12.6 1.0

Reference:

T.Lukk, A.Sakai, C.Kalyanaraman, S.D.Brown, H.J.Imker, L.Song, A.A.Fedorov, E.V.Fedorov, R.Toro, B.Hillerich, R.Seidel, Y.Patskovsky, M.W.Vetting, S.K.Nair, P.C.Babbitt, S.C.Almo, J.A.Gerlt, M.P.Jacobson. Homology Models Guide Discovery of Diverse Enzyme Specificities Among Dipeptide Epimerases in the Enolase Superfamily. Proc.Natl.Acad.Sci.Usa V. 109 4122 2012.
ISSN: ISSN 0027-8424
PubMed: 22392983
DOI: 10.1073/PNAS.1112081109
Page generated: Thu Aug 15 10:15:00 2024

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