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Manganese in PDB 3l6b: X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor

Enzymatic activity of X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor

All present enzymatic activity of X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor:
5.1.1.18;

Protein crystallography data

The structure of X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor, PDB code: 3l6b was solved by M.A.Smith, J.Barker, V.Mack, A.Ebneth, I.Moraes, B.Felicetti, A.Cesura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.11 / 1.50
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 54.570, 84.290, 69.980, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 17.7

Manganese Binding Sites:

The binding sites of Manganese atom in the X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor (pdb code 3l6b). 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 X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor, PDB code: 3l6b:

Manganese binding site 1 out of 1 in 3l6b

Go back to Manganese Binding Sites List in 3l6b
Manganese binding site 1 out of 1 in the X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Crystal Structure of Human Serine Racemase in Complex with Malonate A Potent Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn347

b:11.2
occ:1.00
 OD1 A:ASP216 2.1 5.2 1.0
OE2 A:GLU210 2.1 5.4 1.0
O A:ALA214 2.2 5.4 1.0
O A:HOH392 2.2 11.2 1.0
O A:HOH360 2.2 10.4 1.0
O A:HOH376 2.3 11.2 1.0
CD A:GLU210 3.1 4.6 1.0
CG A:ASP216 3.1 6.0 1.0
C A:ALA214 3.4 4.9 1.0
CG A:GLU210 3.5 4.5 1.0
OD2 A:ASP216 3.7 6.2 1.0
N A:ASP216 3.9 5.0 1.0
CB A:ALA214 4.0 5.1 1.0
O A:VAL240 4.1 5.4 1.0
O A:SER242 4.1 7.0 1.0
O A:VAL184 4.1 4.6 1.0
N A:CYS217 4.2 5.6 1.0
OE1 A:GLU210 4.2 5.5 1.0
N A:ASP215 4.3 5.2 1.0
CA A:ALA214 4.3 5.0 1.0
CB A:ASP216 4.3 5.0 1.0
OD1 A:ASN229 4.4 9.8 1.0
CA A:ASP215 4.5 5.3 1.0
O A:GLY185 4.5 4.9 1.0
C A:ASP215 4.5 5.4 1.0
CA A:ASP216 4.5 5.3 1.0
CB A:CYS217 4.8 6.2 1.0
CA A:GLY185 4.8 4.3 1.0
C A:ASP216 4.9 5.5 1.0
ND2 A:ASN229 4.9 6.9 1.0
CB A:GLU210 4.9 3.9 1.0
C A:VAL184 5.0 4.7 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 16:47:28 2024

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