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Molybdenum in PDB 2ca3: Sulfite Dehydrogenase From Starkeya Novella R55M Mutant

Protein crystallography data

The structure of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant, PDB code: 2ca3 was solved by S.Bailey, U.Kappler, C.Feng, M.J.Honeychurch, P.V.Bernhardt, G.Tollin, J.H.Enemark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.654, 93.321, 56.035, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 20.6

Other elements in 2ca3:

The structure of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant also contains other interesting chemical elements:

Iron (Fe) 1 atom

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Sulfite Dehydrogenase From Starkeya Novella R55M Mutant (pdb code 2ca3). 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 Sulfite Dehydrogenase From Starkeya Novella R55M Mutant, PDB code: 2ca3:

Molybdenum binding site 1 out of 1 in 2ca3

Go back to Molybdenum Binding Sites List in 2ca3
Molybdenum binding site 1 out of 1 in the Sulfite Dehydrogenase From Starkeya Novella R55M Mutant


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Sulfite Dehydrogenase From Starkeya Novella R55M Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo1374

b:38.6
occ:0.50
MOM1 A:MSS1374 0.0 38.6 0.5
OM1 A:MSS1374 1.7 29.6 1.0
S2' A:MSS1374 2.4 16.7 1.0
S1' A:MSS1374 2.4 18.4 1.0
SG A:CYS104 2.8 23.3 1.0
O4 A:SO41375 2.9 39.8 1.0
C1' A:MSS1374 3.2 15.9 1.0
C2' A:MSS1374 3.3 20.0 1.0
CA A:CYS104 3.5 10.8 1.0
CB A:CYS104 3.6 13.9 1.0
N A:SER105 3.6 11.3 1.0
N A:THR211 3.9 13.2 1.0
OH A:TYR236 4.0 22.6 1.0
C A:CYS104 4.1 9.8 1.0
S A:SO41375 4.2 42.3 1.0
CA A:THR211 4.4 12.3 1.0
OG A:SER105 4.4 16.9 1.0
C A:GLY210 4.4 12.3 1.0
CE1 A:TYR236 4.5 18.0 1.0
CB A:THR211 4.5 9.3 1.0
O2 A:SO41375 4.5 34.7 1.0
CB A:SER105 4.5 13.3 1.0
CZ A:TYR236 4.7 19.1 1.0
C6 A:MSS1374 4.7 10.8 1.0
CA A:SER105 4.7 13.2 1.0
CA A:GLY210 4.7 11.7 1.0
N A:CYS104 4.7 10.7 1.0
C3' A:MSS1374 4.7 13.2 1.0
O3 A:SO41375 4.8 37.8 1.0
N A:GLY210 4.9 18.3 1.0
CB A:MET55 4.9 14.8 1.0

Reference:

S.Bailey, T.Rapson, K.Johnson-Winters, A.V.Astashkin, J.H.Enemark, U.Kappler. Molecular Basis For Enzymatic Sulfite Oxidation: How Three Conserved Active Site Residues Shape Enzyme Activity. J.Biol.Chem. V. 284 2053 2009.
ISSN: ISSN 0021-9258
PubMed: 19004819
DOI: 10.1074/JBC.M807718200
Page generated: Tue Dec 15 05:17:03 2020

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