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Manganese in PDB 3l6r: The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding

Enzymatic activity of The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding

All present enzymatic activity of The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding:
5.1.1.18;

Protein crystallography data

The structure of The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding, PDB code: 3l6r was solved by M.A.Smith, V.Mack, A.Ebneth, A.Cesura, B.Felicetti, J.Barker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.78 / 1.70
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.543, 84.212, 70.376, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.2

Manganese Binding Sites:

The binding sites of Manganese atom in the The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding (pdb code 3l6r). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding, PDB code: 3l6r:

Manganese binding site 1 out of 1 in 3l6r

Go back to Manganese Binding Sites List in 3l6r
Manganese binding site 1 out of 1 in the The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn348

b:12.1
occ:1.00
 O A:HOH702 2.1 13.4 1.0
OE2 A:GLU210 2.2 13.6 1.0
O A:HOH696 2.2 11.2 1.0
OD1 A:ASP216 2.2 13.1 1.0
O A:HOH411 2.2 13.6 1.0
O A:ALA214 2.3 13.4 1.0
CD A:GLU210 3.1 11.4 1.0
CG A:ASP216 3.2 15.1 1.0
C A:ALA214 3.4 13.7 1.0
CG A:GLU210 3.6 11.2 1.0
OD2 A:ASP216 3.7 15.3 1.0
N A:ASP216 3.8 12.5 1.0
CB A:ALA214 4.1 13.8 1.0
O A:SER242 4.1 16.3 1.0
O A:VAL184 4.1 12.0 1.0
O A:VAL240 4.1 12.2 1.0
N A:CYS217 4.2 13.0 1.0
N A:ASP215 4.2 14.9 1.0
OE1 A:GLU210 4.2 14.6 1.0
CA A:ALA214 4.3 13.7 1.0
CA A:ASP215 4.3 14.7 1.0
CB A:ASP216 4.3 12.7 1.0
C A:ASP215 4.4 14.5 1.0
ND2 A:ASN229 4.4 14.3 1.0
CA A:ASP216 4.5 12.6 1.0
O A:GLY185 4.5 12.0 1.0
CB A:CYS217 4.8 14.4 1.0
CA A:GLY185 4.9 11.5 1.0
C A:ASP216 4.9 13.9 1.0
CB A:GLU210 4.9 12.9 1.0
OD1 A:ASN229 4.9 19.1 1.0
C A:VAL184 5.0 10.8 1.0

Reference:

M.A.Smith, V.Mack, A.Ebneth, I.Moraes, B.Felicetti, M.Wood, D.Schonfeld, O.Mather, A.Cesura, J.Barker. The Structure of Mammalian Serine Racemase: Evidence For Conformational Changes Upon Inhibitor Binding. J.Biol.Chem. V. 285 12873 2010.
ISSN: ISSN 0021-9258
PubMed: 20106978
DOI: 10.1074/JBC.M109.050062
Page generated: Sat Oct 5 16:48:24 2024

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