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Molybdenum in PDB 3egw: The Crystal Structure of the Narghi Mutant Narh - C16A

Enzymatic activity of The Crystal Structure of the Narghi Mutant Narh - C16A

All present enzymatic activity of The Crystal Structure of the Narghi Mutant Narh - C16A:
1.7.99.4;

Protein crystallography data

The structure of The Crystal Structure of the Narghi Mutant Narh - C16A, PDB code: 3egw was solved by M.G.Bertero, R.A.Rothery, 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) 19.99 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 153.995, 241.684, 139.475, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 19.6

Other elements in 3egw:

The structure of The Crystal Structure of the Narghi Mutant Narh - C16A also contains other interesting chemical elements:

Iron (Fe) 20 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the The Crystal Structure of the Narghi Mutant Narh - C16A (pdb code 3egw). 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 the Narghi Mutant Narh - C16A, PDB code: 3egw:

Molybdenum binding site 1 out of 1 in 3egw

Go back to Molybdenum Binding Sites List in 3egw
Molybdenum binding site 1 out of 1 in the The Crystal Structure of the Narghi Mutant Narh - C16A


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 the Narghi Mutant Narh - C16A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1247

b:21.9
occ:1.00
OD1 A:ASP222 2.0 21.2 1.0
S13 A:MD11245 2.4 18.5 1.0
S12 A:MD11245 2.4 21.6 1.0
S13 A:MGD1246 2.4 20.2 1.0
S12 A:MGD1246 2.4 19.3 1.0
O A:HOH1836 2.5 32.1 1.0
CG A:ASP222 2.7 18.6 1.0
OD2 A:ASP222 2.7 20.9 1.0
C13 A:MGD1246 3.4 17.4 1.0
C12 A:MGD1246 3.5 18.1 1.0
C13 A:MD11245 3.5 18.9 1.0
C12 A:MD11245 3.5 19.2 1.0
N A:GLY579 3.8 16.5 1.0
CA A:GLY579 3.9 16.4 1.0
ND2 A:ASN52 4.0 14.0 1.0
CB A:ASP222 4.1 17.4 1.0
CE1 A:HIS1092 4.2 16.4 1.0
CE1 A:HIS1098 4.3 16.4 1.0
C A:VAL578 4.3 16.7 1.0
CB A:TYR220 4.5 17.7 1.0
CB A:VAL578 4.5 17.5 1.0
CD2 A:TYR220 4.7 19.5 1.0
NE2 A:HIS1098 4.8 16.0 1.0
O A:VAL578 4.9 17.1 1.0
C14 A:MGD1246 4.9 16.4 1.0
C14 A:MD11245 4.9 19.3 1.0
CA A:VAL578 4.9 16.9 1.0
CG A:TYR220 5.0 18.7 1.0
C11 A:MGD1246 5.0 16.3 1.0

Reference:

A.Parkin, C.F.Blanford, R.A.Rothery, R.Macey, M.Bertero, N.C.J.Strynadka, F.A.Armstrong, J.H.Weiner. When Width Is More Important Than Height: Barriers to Electron Transfer in E.Coli Nitrate Reductase To Be Published.
Page generated: Mon Jan 25 15:37:34 2021

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