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Manganese in PDB 1dck: Structure of Unphosphorylated Fixj-N Complexed with MN2+

Protein crystallography data

The structure of Structure of Unphosphorylated Fixj-N Complexed with MN2+, PDB code: 1dck was solved by P.Gouet, B.Fabry, V.Guillet, C.Birck, L.Mourey, D.Kahn, J.P.Samama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.45 / 2.00
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 31.700, 42.500, 44.700, 93.20, 103.00, 101.80
R / Rfree (%) 20.6 / 25.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Structure of Unphosphorylated Fixj-N Complexed with MN2+ (pdb code 1dck). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Structure of Unphosphorylated Fixj-N Complexed with MN2+, PDB code: 1dck:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in 1dck

Go back to Manganese Binding Sites List in 1dck
Manganese binding site 1 out of 3 in the Structure of Unphosphorylated Fixj-N Complexed with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Unphosphorylated Fixj-N Complexed with MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1001

b:42.5
occ:1.00
O A:ARG56 2.4 36.4 1.0
OD1 A:ASP11 2.4 41.3 1.0
O A:HOH1003 2.5 37.9 1.0
OD1 A:ASP54 2.5 33.1 1.0
O A:HOH1004 2.7 36.3 1.0
CG A:ASP54 3.4 32.4 1.0
CG A:ASP11 3.4 39.7 1.0
C A:ARG56 3.5 35.2 1.0
OD2 A:ASP11 3.8 40.0 1.0
OD2 A:ASP54 3.8 34.1 1.0
CB A:ARG56 4.3 35.7 1.0
OD1 A:ASP10 4.3 39.1 1.0
CA A:ARG56 4.3 35.6 1.0
OE1 A:GLU12 4.4 40.9 1.0
NZ A:LYS104 4.5 32.7 1.0
N A:MET57 4.5 36.6 1.0
CB A:ASP54 4.5 31.6 1.0
CG A:MET57 4.5 35.1 1.0
N A:ARG56 4.6 34.1 1.0
CG A:GLU12 4.6 39.4 1.0
CA A:MET57 4.7 36.5 1.0
CB A:ASP11 4.7 38.1 1.0
CD A:GLU12 5.0 41.3 1.0

Manganese binding site 2 out of 3 in 1dck

Go back to Manganese Binding Sites List in 1dck
Manganese binding site 2 out of 3 in the Structure of Unphosphorylated Fixj-N Complexed with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Unphosphorylated Fixj-N Complexed with MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1002

b:30.9
occ:1.00
O B:ARG56 2.3 23.8 1.0
O B:HOH1004 2.4 33.3 1.0
O B:HOH1005 2.4 19.7 1.0
OD1 B:ASP11 2.4 27.3 1.0
O B:HOH1006 2.4 26.3 1.0
OD2 B:ASP54 2.4 26.4 1.0
CG B:ASP54 3.2 25.1 1.0
CG B:ASP11 3.3 27.2 1.0
OD2 B:ASP11 3.5 30.6 1.0
C B:ARG56 3.5 24.7 1.0
OD1 B:ASP54 3.5 27.8 1.0
OE1 B:GLU12 3.7 37.4 1.0
OD2 B:ASP10 3.9 29.1 1.0
CD B:GLU12 4.3 35.7 1.0
CA B:ARG56 4.3 24.8 1.0
CG B:MET57 4.3 25.4 1.0
CB B:ASP54 4.3 22.0 1.0
CB B:ARG56 4.4 27.6 1.0
N B:MET57 4.5 24.7 1.0
O B:HOH1007 4.5 27.5 1.0
N B:ARG56 4.6 22.6 1.0
CG B:GLU12 4.6 31.8 1.0
CA B:MET57 4.7 27.2 1.0
CB B:ASP11 4.7 26.0 1.0
O B:HOH1034 4.7 39.0 1.0
N B:ASP11 4.8 21.6 1.0
CG B:ASP10 4.9 27.5 1.0

Manganese binding site 3 out of 3 in 1dck

Go back to Manganese Binding Sites List in 1dck
Manganese binding site 3 out of 3 in the Structure of Unphosphorylated Fixj-N Complexed with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Structure of Unphosphorylated Fixj-N Complexed with MN2+ within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1003

b:47.1
occ:1.00
NE2 B:HIS84 2.4 26.3 1.0
CE1 B:HIS84 3.2 27.6 1.0
CD2 B:HIS84 3.5 23.9 1.0
ND1 B:HIS84 4.4 26.7 1.0
CG B:HIS84 4.6 25.6 1.0

Reference:

P.Gouet, B.Fabry, V.Guillet, C.Birck, L.Mourey, D.Kahn, J.P.Samama. Structural Transitions in the Fixj Receiver Domain. Structure Fold.Des. V. 7 1517 1999.
ISSN: ISSN 0969-2126
PubMed: 10647182
DOI: 10.1016/S0969-2126(00)88342-2
Page generated: Sat Oct 5 10:05:32 2024

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