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Manganese in PDB 2p7o: Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form)

Protein crystallography data

The structure of Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form), PDB code: 2p7o was solved by K.L.Fillgrove, S.Pakhomova, M.Schaab, 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) 10.00 / 1.44
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 68.579, 68.579, 56.835, 90.00, 90.00, 90.00
R / Rfree (%) 12.4 / 16.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form) (pdb code 2p7o). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form), PDB code: 2p7o:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 2p7o

Go back to Manganese Binding Sites List in 2p7o
Manganese binding site 1 out of 2 in the Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form)


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 Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn6000

b:18.5
occ:1.00
OE1 A:GLU126 2.1 16.5 1.0
NE2 A:HIS69 2.1 17.3 1.0
OE1 A:GLU118 2.2 15.2 1.0
O A:HOH7005 2.2 15.8 1.0
NE2 B:HIS7 2.2 16.5 1.0
CD A:GLU126 2.8 17.0 1.0
OE2 A:GLU126 3.0 19.8 1.0
CE1 A:HIS69 3.1 15.6 1.0
CE1 B:HIS7 3.1 16.8 1.0
CD2 A:HIS69 3.1 16.5 1.0
CD A:GLU118 3.2 17.8 1.0
OH A:TYR108 3.3 28.9 1.0
CD2 B:HIS7 3.3 17.5 1.0
OE2 A:GLU118 3.6 17.5 1.0
OG1 B:THR9 3.8 17.2 1.0
CZ A:TYR108 4.2 22.6 1.0
CA A:GLU126 4.2 17.2 1.0
ND1 A:HIS69 4.2 15.7 1.0
CE2 A:TYR108 4.2 19.0 1.0
CG A:GLU126 4.3 17.7 1.0
CG A:HIS69 4.3 14.7 1.0
ND1 B:HIS7 4.3 16.1 1.0
CG B:HIS7 4.4 17.0 1.0
N A:ARG127 4.4 19.6 1.0
CB A:ALA71 4.5 20.6 1.0
CG A:GLU118 4.5 18.9 1.0
O A:GLU125 4.6 17.6 1.0
CB A:GLU126 4.6 16.2 1.0
CB B:THR9 4.6 16.3 1.0
CB A:GLU118 4.8 17.4 1.0
C A:GLU126 4.9 20.6 1.0

Manganese binding site 2 out of 2 in 2p7o

Go back to Manganese Binding Sites List in 2p7o
Manganese binding site 2 out of 2 in the Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form)


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes (Tetragonal Form) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn4000

b:17.1
occ:1.00
OE1 B:GLU118 2.0 20.3 1.0
NE2 A:HIS7 2.2 17.3 1.0
OE1 B:GLU126 2.2 21.8 1.0
O B:HOH7001 2.3 18.6 1.0
NE2 B:HIS69 2.3 17.2 1.0
CD B:GLU126 3.0 21.7 1.0
CE1 A:HIS7 3.1 18.8 1.0
CD B:GLU118 3.1 18.3 1.0
OE2 B:GLU126 3.1 31.3 1.0
CD2 A:HIS7 3.2 19.1 1.0
CE1 B:HIS69 3.3 18.2 1.0
CD2 B:HIS69 3.3 17.9 1.0
OH B:TYR108 3.4 20.9 1.0
OE2 B:GLU118 3.4 18.6 1.0
OG1 A:THR9 3.8 17.9 1.0
CZ B:TYR108 4.2 19.2 1.0
ND1 A:HIS7 4.2 18.1 1.0
CE2 B:TYR108 4.3 22.2 1.0
CG A:HIS7 4.3 16.1 1.0
CA B:GLU126 4.3 19.6 1.0
O B:GLU125 4.4 22.8 1.0
CG B:GLU126 4.4 19.1 1.0
ND1 B:HIS69 4.4 17.9 1.0
CG B:GLU118 4.4 17.7 1.0
CG B:HIS69 4.5 18.1 1.0
N B:ARG127 4.5 16.8 1.0
CB B:ALA71 4.5 16.3 1.0
CB A:THR9 4.6 19.1 1.0
CB B:GLU118 4.7 18.2 1.0
CB B:GLU126 4.8 21.6 1.0

Reference:

K.L.Fillgrove, S.Pakhomova, M.R.Schaab, M.E.Newcomer, R.N.Armstrong. Structure and Mechanism of the Genomically Encoded Fosfomycin Resistance Protein, Fosx, From Listeria Monocytogenes. Biochemistry V. 46 8110 2007.
ISSN: ISSN 0006-2960
PubMed: 17567049
DOI: 10.1021/BI700625P
Page generated: Tue Dec 15 04:04:19 2020

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