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Iron in PDB 1uog: Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C

Enzymatic activity of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C

All present enzymatic activity of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C:
1.14.20.1;

Protein crystallography data

The structure of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C, PDB code: 1uog was solved by K.Valegard, A.C.Terwisscha Van Scheltinga, A.Dubus, L.M.Oster, G.Rhangino, J.Hajdu, I.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.40 / 1.70
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 106.600, 106.600, 74.000, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 24.2

Iron Binding Sites:

The binding sites of Iron atom in the Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C (pdb code 1uog). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C, PDB code: 1uog:

Iron binding site 1 out of 1 in 1uog

Go back to Iron Binding Sites List in 1uog
Iron binding site 1 out of 1 in the Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Deacetoxycephalosporin C Synthase Complexed with Deacetoxycephalosporin C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1312

b:82.5
occ:1.00
NE2 A:HIS243 1.9 36.3 1.0
NE2 A:HIS183 2.1 36.5 1.0
OD1 A:ASP185 2.1 29.6 1.0
C37 A:P1C1311 2.5 44.1 1.0
CD2 A:HIS183 2.6 26.2 1.0
CD2 A:HIS243 2.6 38.9 1.0
S A:P1C1311 2.8 67.0 1.0
CE1 A:HIS243 3.0 36.5 1.0
CG A:ASP185 3.0 30.4 1.0
C16 A:P1C1311 3.1 69.3 1.0
OD2 A:ASP185 3.1 26.0 1.0
CE1 A:HIS183 3.3 33.7 1.0
C32 A:P1C1311 3.3 57.3 1.0
N29 A:P1C1311 3.5 72.8 1.0
C30 A:P1C1311 3.7 66.4 1.0
CG A:HIS243 3.8 37.0 1.0
CG A:HIS183 3.8 25.5 1.0
ND1 A:HIS243 4.0 33.6 1.0
ND1 A:HIS183 4.1 33.0 1.0
CG2 A:ILE305 4.2 25.3 1.0
C33 A:P1C1311 4.4 59.0 1.0
CB A:ASP185 4.4 22.3 1.0
O A:HIS183 4.6 26.1 1.0
CD2 A:PHE225 4.6 40.9 1.0
N A:ASP185 4.6 20.9 1.0
C12 A:P1C1311 4.6 64.0 1.0
C13 A:P1C1311 4.8 71.3 1.0
C A:TYR184 4.8 21.7 1.0
CA A:ASP185 4.8 21.3 1.0
CE2 A:PHE225 4.8 35.6 1.0
C31 A:P1C1311 4.8 70.0 1.0
O A:TYR184 5.0 18.9 1.0

Reference:

K.Valegard, A.C.Terwisscha Van Scheltinga, A.Dubus, G.Ranghino, L.M.Oster, J.Hajdu, I.Andersson. The Structural Basis of Cephalosporin Formation in A Mononuclear Ferrous Enzyme Nat.Struct.Mol.Biol. V. 11 95 2004.
ISSN: ISSN 1545-9993
PubMed: 14718929
DOI: 10.1038/NSMB712
Page generated: Sun Dec 13 14:33:41 2020

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