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Manganese in PDB 1lqk: High Resolution Structure of Fosfomycin Resistance Protein A (Fosa)

Enzymatic activity of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa)

All present enzymatic activity of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa):
2.5.1.18;

Protein crystallography data

The structure of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa), PDB code: 1lqk was solved by C.L.Rife, R.E.Pharris, M.E.Newcomer, R.N.Armstrong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.35
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.788, 66.967, 77.000, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 18.5

Other elements in 1lqk:

The structure of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa) also contains other interesting chemical elements:

Potassium (K) 2 atoms

Manganese Binding Sites:

The binding sites of Manganese atom in the High Resolution Structure of Fosfomycin Resistance Protein A (Fosa) (pdb code 1lqk). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the High Resolution Structure of Fosfomycin Resistance Protein A (Fosa), PDB code: 1lqk:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1lqk

Go back to Manganese Binding Sites List in 1lqk
Manganese binding site 1 out of 2 in the High Resolution Structure of Fosfomycin Resistance Protein A (Fosa)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn901

b:15.5
occ:0.75
O3 A:PO4501 1.8 16.1 0.6
O3 A:PO4501 1.9 9.5 0.3
OE1 A:GLU110 2.1 8.5 1.0
NE2 A:HIS64 2.1 11.3 1.0
NE2 B:HIS7 2.2 10.5 1.0
P A:PO4501 2.5 13.8 0.6
O4 A:PO4501 2.9 15.9 0.6
O2 A:PO4501 3.0 13.9 0.6
CE1 A:HIS64 3.0 11.1 1.0
CD A:GLU110 3.1 8.2 1.0
CD2 A:HIS64 3.1 10.9 1.0
CE1 B:HIS7 3.2 10.3 1.0
CD2 B:HIS7 3.3 10.1 1.0
O A:HOH1057 3.3 24.3 1.0
P A:PO4501 3.3 12.9 0.3
OE2 A:GLU110 3.5 10.0 1.0
O1 A:PO4501 3.8 22.5 0.3
O1 A:PO4501 3.9 15.6 0.6
OG1 B:THR9 4.0 10.1 1.0
O2 A:PO4501 4.2 19.2 0.3
ND1 A:HIS64 4.2 10.5 1.0
CG A:HIS64 4.3 10.2 1.0
CE2 A:TYR100 4.3 10.7 1.0
ND1 B:HIS7 4.3 9.7 1.0
CG B:HIS7 4.4 8.6 1.0
O4 A:PO4501 4.4 29.6 0.3
CB A:ALA66 4.5 8.4 1.0
CG A:GLU110 4.5 7.9 1.0
OH A:TYR100 4.6 14.8 1.0
CB A:GLU110 4.8 7.6 1.0
CZ A:TYR100 5.0 11.4 1.0

Manganese binding site 2 out of 2 in 1lqk

Go back to Manganese Binding Sites List in 1lqk
Manganese binding site 2 out of 2 in the High Resolution Structure of Fosfomycin Resistance Protein A (Fosa)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of High Resolution Structure of Fosfomycin Resistance Protein A (Fosa) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn801

b:15.6
occ:0.70
O1 B:PO4401 1.7 15.8 0.3
O3 B:PO4401 1.8 15.9 0.6
NE2 B:HIS64 2.1 11.9 1.0
OE1 B:GLU110 2.2 9.5 1.0
NE2 A:HIS7 2.2 11.0 1.0
P B:PO4401 2.5 13.2 0.6
O1 B:PO4401 2.8 11.1 0.6
CE1 B:HIS64 3.0 11.9 1.0
O4 B:PO4401 3.1 12.1 0.6
CE1 A:HIS7 3.2 9.1 1.0
CD2 B:HIS64 3.2 11.4 1.0
P B:PO4401 3.2 12.4 0.3
CD B:GLU110 3.2 8.6 1.0
O B:HOH978 3.3 22.3 1.0
CD2 A:HIS7 3.3 10.6 1.0
OE2 B:GLU110 3.5 10.3 1.0
O3 B:PO4401 3.8 18.3 0.3
O2 B:PO4401 3.9 13.4 0.6
OG1 A:THR9 4.0 10.0 1.0
O2 B:PO4401 4.0 23.0 0.3
O4 B:PO4401 4.1 15.7 0.3
ND1 B:HIS64 4.1 10.4 1.0
CG B:HIS64 4.3 9.9 1.0
ND1 A:HIS7 4.3 8.9 1.0
CE2 B:TYR100 4.4 12.2 1.0
CG A:HIS7 4.4 9.2 1.0
CG B:GLU110 4.5 8.7 1.0
CB B:ALA66 4.5 9.3 1.0
OH B:TYR100 4.8 13.2 1.0
CB B:GLU110 4.8 8.9 1.0
CB A:THR9 4.9 9.0 1.0

Reference:

C.L.Rife, R.E.Pharris, M.E.Newcomer, R.N.Armstrong. Crystal Structure of A Genomically Encoded Fosfomycin Resistance Protein (Fosa) at 1.19 A Resolution By Mad Phasing Off the L-III Edge of Tl(+) J.Am.Chem.Soc. V. 124 11001 2002.
ISSN: ISSN 0002-7863
PubMed: 12224946
DOI: 10.1021/JA026879V
Page generated: Tue Dec 15 03:52:11 2020

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