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Molybdenum in PDB 1y4z: The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol

Enzymatic activity of The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol

All present enzymatic activity of The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol:
1.7.99.4;

Protein crystallography data

The structure of The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol, PDB code: 1y4z was solved by M.G.Bertero, R.A.Rothery, N.Boroumand, M.Palak, F.Blasco, N.Ginet, J.H.Weiner, N.C.J.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.75 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 154.456, 241.342, 140.014, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 23.3

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol (pdb code 1y4z). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol, PDB code: 1y4z:

Molybdenum binding site 1 out of 1 in 1y4z

Go back to Molybdenum Binding Sites List in 1y4z
Molybdenum binding site 1 out of 1 in the The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of The Crystal Structure of Nitrate Reductase A, Narghi, in Complex with the Q-Site Inhibitor Pentachlorophenol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo3800

b:52.7
occ:1.00
OD1 A:ASP222 2.1 40.9 1.0
OD2 A:ASP222 2.3 42.6 1.0
S13 A:MD11800 2.4 32.9 1.0
S13 A:MD12800 2.4 39.9 1.0
CG A:ASP222 2.5 37.7 1.0
S12 A:MD11800 2.5 40.8 1.0
S12 A:MD12800 2.6 36.1 1.0
C13 A:MD12800 3.5 33.7 1.0
N A:GLY579 3.5 34.9 1.0
C13 A:MD11800 3.6 31.4 1.0
C12 A:MD12800 3.6 33.9 1.0
C12 A:MD11800 3.6 36.9 1.0
CA A:GLY579 3.6 34.3 1.0
CB A:ASP222 4.0 34.0 1.0
ND2 A:ASN52 4.1 30.8 1.0
C A:VAL578 4.2 34.5 1.0
CE1 A:HIS1092 4.2 27.9 1.0
CE1 A:HIS1098 4.3 28.1 1.0
CB A:VAL578 4.4 34.5 1.0
CB A:TYR220 4.5 32.2 1.0
CD2 A:TYR220 4.7 38.3 1.0
O A:VAL578 4.8 33.2 1.0
NE2 A:HIS1098 4.8 27.9 1.0
CA A:VAL578 4.8 33.3 1.0
CA A:ASP222 4.9 28.7 1.0
C14 A:MD12800 4.9 28.4 1.0
C14 A:MD11800 4.9 29.1 1.0

Reference:

M.G.Bertero, R.A.Rothery, N.Boroumand, M.Palak, F.Blasco, N.Ginet, J.H.Weiner, N.C.J.Strynadka. Structural and Biochemical Characterization of A Quinol Binding Site of Escherichia Coli Nitrate Reductase A J.Biol.Chem. V. 280 14836 2005.
ISSN: ISSN 0021-9258
PubMed: 15615728
DOI: 10.1074/JBC.M410457200
Page generated: Wed Sep 23 13:32:28 2020
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