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Iron in PDB 2bu9: Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline

Enzymatic activity of Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline

All present enzymatic activity of Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline:
1.21.3.1;

Protein crystallography data

The structure of Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline, PDB code: 2bu9 was solved by A.R.Howard-Jones, P.J.Rutledge, I.J.Clifton, R.M.Adlington, J.E.Baldwin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.03 / 1.3
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.465, 71.012, 100.768, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 16.8

Other elements in 2bu9:

The structure of Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline also contains other interesting chemical elements:

Fluorine (F) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline (pdb code 2bu9). 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 Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline, PDB code: 2bu9:

Iron binding site 1 out of 1 in 2bu9

Go back to Iron Binding Sites List in 2bu9
Iron binding site 1 out of 1 in the Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Isopenicillin N Synthase Complexed with L-Aminoadipoyl-L- Cysteinyl-L-Hexafluorovaline within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1332

b:6.1
occ:1.00
 OD1 A:ASP216 2.1 12.4 1.0
NE2 A:HIS214 2.2 11.3 1.0
O A:HOH2337 2.2 7.6 1.0
O A:HOH2463 2.2 7.4 1.0
NE2 A:HIS270 2.2 11.4 1.0
S17 A:HFV1333 2.5 7.2 1.0
CE1 A:HIS270 3.1 12.3 1.0
CG A:ASP216 3.1 13.1 1.0
CE1 A:HIS214 3.2 12.1 1.0
CD2 A:HIS214 3.2 11.6 1.0
CD2 A:HIS270 3.3 12.3 1.0
C16 A:HFV1333 3.4 7.1 1.0
OD2 A:ASP216 3.5 13.5 1.0
O A:HOH2150 3.9 15.0 1.0
O A:HOH2151 4.0 20.7 1.0
ND1 A:HIS270 4.3 12.2 1.0
ND1 A:HIS214 4.3 12.4 1.0
CG A:HIS214 4.3 10.9 1.0
CG A:HIS270 4.3 12.8 1.0
CB A:ASP216 4.4 12.0 1.0
O A:HOH2376 4.5 16.8 1.0
O43 A:HFV1333 4.5 13.4 1.0
O A:HOH2338 4.7 9.2 1.0
CA A:ASP216 4.7 11.8 1.0
C12 A:HFV1333 4.8 7.7 1.0
N A:ASP216 5.0 12.1 1.0

Reference:

A.R.Howard-Jones, P.J.Rutledge, I.J.Clifton, R.M.Adlington, J.E.Baldwin. Unique Binding of A Non-Natural L,L,L-Substrate By Isopenicillin N Synthase Biochem.Biophys.Res.Commun. V. 336 702 2005.
ISSN: ISSN 0006-291X
PubMed: 16143309
DOI: 10.1016/J.BBRC.2005.08.155
Page generated: Sat Aug 3 19:48:32 2024

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