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Molybdenum in PDB 1h9s: Molybdate Bound Complex of Dimop Domain of Mode From E.Coli

Protein crystallography data

The structure of Molybdate Bound Complex of Dimop Domain of Mode From E.Coli, PDB code: 1h9s was solved by D.G.Gourley, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.0 / 1.82
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 72.340, 73.340, 49.560, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 23.4

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Molybdate Bound Complex of Dimop Domain of Mode From E.Coli (pdb code 1h9s). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Molybdate Bound Complex of Dimop Domain of Mode From E.Coli, PDB code: 1h9s:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1h9s

Go back to Molybdenum Binding Sites List in 1h9s
Molybdenum binding site 1 out of 2 in the Molybdate Bound Complex of Dimop Domain of Mode From E.Coli


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Molybdate Bound Complex of Dimop Domain of Mode From E.Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1261

b:16.3
occ:1.00
MO A:MOO1261 0.0 16.3 1.0
O2 A:MOO1261 1.7 25.3 1.0
O3 A:MOO1261 1.7 23.7 1.0
O4 A:MOO1261 1.7 24.9 1.0
O1 A:MOO1261 1.7 26.4 1.0
O A:SER126 3.0 25.7 1.0
CG A:LYS183 3.6 26.3 1.0
NZ A:LYS183 3.7 25.7 1.0
C A:SER126 3.8 28.0 1.0
N B:THR163 3.9 25.9 1.0
CE A:LYS183 4.1 26.1 1.0
CG2 B:THR163 4.2 27.0 1.0
N A:ALA184 4.2 25.2 1.0
OG A:SER126 4.2 27.6 1.0
N A:ARG128 4.2 25.9 1.0
CG A:ARG128 4.2 27.0 1.0
CB A:SER126 4.2 27.7 1.0
CA B:ILE162 4.2 26.6 1.0
CA A:ALA127 4.2 28.5 1.0
OG B:SER166 4.3 30.1 1.0
OG1 B:THR163 4.3 24.9 1.0
CB A:ALA184 4.4 26.9 1.0
N A:ALA127 4.4 27.8 1.0
CB B:ILE162 4.5 27.2 1.0
O A:HOH2097 4.5 26.6 1.0
C B:ILE162 4.6 26.4 1.0
CD A:LYS183 4.6 27.5 1.0
CA A:SER126 4.6 27.8 1.0
C A:ALA127 4.7 28.7 1.0
CD A:PRO185 4.7 27.1 1.0
CB B:THR163 4.7 26.4 1.0
CA A:LYS183 4.7 25.6 1.0
CB A:LYS183 4.7 27.1 1.0
CB B:SER166 4.8 28.4 1.0
CA B:THR163 4.9 27.6 1.0
CB A:ARG128 4.9 25.0 1.0
CA A:ALA184 4.9 25.3 1.0
CG2 B:ILE162 4.9 26.5 1.0
C A:LYS183 5.0 25.2 1.0

Molybdenum binding site 2 out of 2 in 1h9s

Go back to Molybdenum Binding Sites List in 1h9s
Molybdenum binding site 2 out of 2 in the Molybdate Bound Complex of Dimop Domain of Mode From E.Coli


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Molybdate Bound Complex of Dimop Domain of Mode From E.Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mo1261

b:17.1
occ:1.00
MO B:MOO1261 0.0 17.1 1.0
O3 B:MOO1261 1.6 25.5 1.0
O4 B:MOO1261 1.6 28.9 1.0
O2 B:MOO1261 1.7 30.2 1.0
O1 B:MOO1261 1.7 28.9 1.0
O B:SER126 3.1 28.2 1.0
CG B:LYS183 3.6 28.4 1.0
C B:SER126 3.8 29.0 1.0
NZ B:LYS183 3.8 24.7 1.0
N A:THR163 3.9 26.5 1.0
N B:ALA184 4.1 26.0 1.0
N B:ARG128 4.2 28.5 1.0
CG2 A:THR163 4.2 28.1 1.0
CG B:ARG128 4.2 28.0 1.0
CA B:ALA127 4.2 27.4 1.0
CA A:ILE162 4.3 26.6 1.0
OG A:SER166 4.3 28.1 1.0
OG B:SER126 4.3 29.0 1.0
CE B:LYS183 4.3 28.7 1.0
OG1 A:THR163 4.3 27.3 1.0
CB B:SER126 4.3 28.6 1.0
O B:HOH2109 4.4 28.7 1.0
N B:ALA127 4.4 28.4 1.0
CB A:ILE162 4.4 28.7 1.0
CB B:ALA184 4.5 26.8 1.0
C A:ILE162 4.6 26.6 1.0
CD B:LYS183 4.6 27.1 1.0
CD B:PRO185 4.6 26.0 1.0
C B:ALA127 4.7 29.5 1.0
CA B:SER126 4.7 28.2 1.0
CB A:THR163 4.7 28.6 1.0
CB A:SER166 4.7 27.4 1.0
CB B:LYS183 4.8 27.9 1.0
CA B:LYS183 4.8 27.9 1.0
CG2 A:ILE162 4.8 28.9 1.0
CA A:THR163 4.9 27.3 1.0
CB B:ARG128 4.9 27.9 1.0
CA B:ALA184 4.9 26.5 1.0
C B:LYS183 4.9 27.4 1.0

Reference:

D.G.Gourley, A.W.Schuttelkopf, L.A.Anderson, N.C.Price, D.H.Boxer, W.N.Hunter. Oxyanion Binding Alters Conformational and Quaternary Structure of the C-Terminal Domain of the Transcriptional Regulator Mode; Implications For Molybdate-Dependant Regulation, Signalling, Storage and Transport J.Biol.Chem. V. 276 20641 2001.
ISSN: ISSN 0021-9258
PubMed: 11259434
DOI: 10.1074/JBC.M100919200
Page generated: Tue Dec 15 05:15:37 2020

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