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Manganese in PDB 2vqr: Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily

Protein crystallography data

The structure of Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily, PDB code: 2vqr was solved by S.Jonas, M.Hyvonen, F.Hollfelder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.63 / 1.42
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 59.700, 96.600, 178.500, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 18.2

Other elements in 2vqr:

The structure of Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily also contains other interesting chemical elements:

Calcium (Ca) 1 atom
Sodium (Na) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily (pdb code 2vqr). 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 Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily, PDB code: 2vqr:

Manganese binding site 1 out of 1 in 2vqr

Go back to Manganese Binding Sites List in 2vqr
Manganese binding site 1 out of 1 in the Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of A Phosphonate Monoester Hydrolase From Rhizobium Leguminosarum: A New Member of the Alkaline Phosphatase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1515

b:7.8
occ:0.20
CA A:CA1516 0.0 8.4 0.4
OD2 A:ASP324 2.1 12.9 1.0
OG2 A:CYS57 2.1 23.9 0.6
NE2 A:HIS325 2.3 10.7 1.0
OD1 A:ASP12 2.4 12.9 1.0
OD2 A:ASP12 2.5 12.5 1.0
CG A:ASP12 2.7 14.6 1.0
CG A:ASP324 3.0 11.4 1.0
CE1 A:HIS325 3.1 13.5 1.0
CB A:CYS57 3.2 13.3 0.6
SG A:CYS57 3.2 32.2 0.4
CD2 A:HIS325 3.2 10.1 1.0
OD1 A:ASP324 3.2 9.5 1.0
OG1 A:CYS57 3.5 17.0 0.6
CA A:CYS57 3.7 18.9 0.4
CA A:CYS57 3.7 8.9 0.6
O A:HOH2011 3.7 28.3 1.0
CB A:CYS57 3.8 16.5 0.4
CB A:ASP12 4.1 12.3 1.0
ND1 A:HIS325 4.1 9.2 1.0
N A:CYS57 4.1 16.8 0.4
NH2 A:ARG61 4.2 10.6 1.0
CG A:HIS325 4.2 10.3 1.0
N A:CYS57 4.2 5.7 0.6
CD2 A:HIS218 4.3 13.5 1.0
CB A:ASP324 4.3 8.5 1.0
OE1 A:GLN13 4.3 11.8 1.0
NE A:ARG61 4.4 9.6 1.0
NZ A:LYS337 4.4 13.7 1.0
CE A:LYS337 4.5 13.2 1.0
CA A:ASP12 4.6 10.4 1.0
N A:GLN13 4.7 8.5 1.0
O A:HOH2124 4.8 23.6 1.0
CZ A:ARG61 4.8 9.6 1.0
C A:CYS57 4.9 14.9 0.4
C A:ASP12 5.0 7.6 1.0
O A:HOH2333 5.0 40.0 1.0
NE2 A:HIS218 5.0 12.7 1.0

Reference:

S.Jonas, B.Van Loo, M.Hyvonen, F.Hollfelder. A New Member of the Alkaline Phosphatase Superfamily with A Formylglycine Nucleophile: Structural and Kinetic Characterisation of A Phosphonate Monoester Hydrolase/Phosphodiesterase From Rhizobium Leguminosarum. J.Mol.Biol. V. 384 120 2008.
ISSN: ISSN 0022-2836
PubMed: 18793651
DOI: 10.1016/J.JMB.2008.08.072
Page generated: Tue Dec 15 04:05:57 2020

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