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Manganese in PDB 3mmr: Structure of Plasmodium Falciparum Arginase in Complex with Abh

Enzymatic activity of Structure of Plasmodium Falciparum Arginase in Complex with Abh

All present enzymatic activity of Structure of Plasmodium Falciparum Arginase in Complex with Abh:
3.5.3.1;

Protein crystallography data

The structure of Structure of Plasmodium Falciparum Arginase in Complex with Abh, PDB code: 3mmr was solved by D.P.Dowling, M.Ilies, K.L.Olszewski, S.Portugal, M.M.Mota, M.Llinas, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.11 / 2.14
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 112.594, 112.594, 228.900, 90.00, 90.00, 120.00
R / Rfree (%) 15.5 / 18.6

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Plasmodium Falciparum Arginase in Complex with Abh (pdb code 3mmr). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Plasmodium Falciparum Arginase in Complex with Abh, PDB code: 3mmr:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3mmr

Go back to Manganese Binding Sites List in 3mmr
Manganese binding site 1 out of 2 in the Structure of Plasmodium Falciparum Arginase in Complex with Abh


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Plasmodium Falciparum Arginase in Complex with Abh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn412

b:21.2
occ:1.00
OD1 A:ASP216 2.1 21.4 1.0
OD2 A:ASP220 2.1 23.5 1.0
ND1 A:HIS193 2.2 21.4 1.0
O1 A:ABH551 2.2 25.7 1.0
OD2 A:ASP323 2.3 19.0 1.0
O2 A:ABH551 2.4 25.3 1.0
B A:ABH551 2.8 29.5 1.0
CG A:ASP220 3.1 25.3 1.0
CG A:ASP216 3.1 23.3 1.0
CE1 A:HIS193 3.2 21.7 1.0
CG A:HIS193 3.2 20.2 1.0
MN A:MN413 3.3 21.6 1.0
CG A:ASP323 3.3 22.3 1.0
OD1 A:ASP220 3.4 25.5 1.0
OD2 A:ASP216 3.4 21.8 1.0
CB A:HIS193 3.5 21.7 1.0
CB A:ASP323 3.6 17.6 1.0
O3 A:ABH551 3.7 29.4 1.0
CE A:ABH551 4.1 31.1 1.0
NE2 A:HIS193 4.3 21.5 1.0
CD2 A:HIS193 4.3 21.3 1.0
NE1 A:TRP214 4.4 20.4 1.0
OD1 A:ASP323 4.4 18.2 1.0
CB A:ASP216 4.4 20.6 1.0
CB A:ASP220 4.5 20.6 1.0
CZ2 A:TRP214 4.6 20.8 1.0
O A:HIS233 4.6 28.6 1.0
CG A:GLU368 4.7 25.6 1.0
OE2 A:GLU368 4.8 28.6 1.0
CE2 A:TRP214 4.8 23.6 1.0
CA A:HIS193 4.9 23.0 1.0

Manganese binding site 2 out of 2 in 3mmr

Go back to Manganese Binding Sites List in 3mmr
Manganese binding site 2 out of 2 in the Structure of Plasmodium Falciparum Arginase in Complex with Abh


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Plasmodium Falciparum Arginase in Complex with Abh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn413

b:21.6
occ:1.00
O1 A:ABH551 2.2 25.7 1.0
OD2 A:ASP216 2.2 21.8 1.0
ND1 A:HIS218 2.3 22.1 1.0
OD2 A:ASP325 2.3 22.2 1.0
OD2 A:ASP323 2.3 19.0 1.0
OD1 A:ASP325 2.5 20.9 1.0
O3 A:ABH551 2.7 29.4 1.0
CG A:ASP325 2.7 24.6 1.0
B A:ABH551 3.0 29.5 1.0
CE1 A:HIS218 3.1 23.1 1.0
CG A:ASP323 3.1 22.3 1.0
CG A:ASP216 3.1 23.3 1.0
MN A:MN412 3.3 21.2 1.0
CG A:HIS218 3.4 25.0 1.0
OD1 A:ASP216 3.4 21.4 1.0
OD1 A:ASP323 3.7 18.2 1.0
CB A:HIS218 3.8 23.2 1.0
O2 A:ABH551 3.8 25.3 1.0
N A:HIS218 4.1 21.6 1.0
CB A:ASP323 4.2 17.6 1.0
CE A:ABH551 4.2 31.1 1.0
CB A:ASP325 4.2 18.7 1.0
N A:ALA217 4.2 20.7 1.0
NE2 A:HIS218 4.3 25.9 1.0
CD2 A:HIS218 4.4 25.8 1.0
CD A:ABH551 4.4 29.1 1.0
CB A:ASP216 4.5 20.6 1.0
OD1 A:ASP220 4.6 25.5 1.0
CA A:HIS218 4.6 24.1 1.0
O A:HOH416 4.7 24.1 1.0
CB A:ALA217 4.8 17.9 1.0
OD2 A:ASP220 4.8 23.5 1.0
CA A:ASP216 4.8 20.3 1.0
CA A:ALA217 4.9 20.0 1.0
C A:ALA217 4.9 20.6 1.0
C A:ASP216 5.0 21.0 1.0

Reference:

D.P.Dowling, M.Ilies, K.L.Olszewski, S.Portugal, M.M.Mota, M.Llinas, D.W.Christianson. Crystal Structure of Arginase From Plasmodium Falciparum and Implications For L-Arginine Depletion in Malarial Infection . Biochemistry V. 49 5600 2010.
ISSN: ISSN 0006-2960
PubMed: 20527960
DOI: 10.1021/BI100390Z
Page generated: Tue Dec 15 04:12:31 2020

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