Atomistry » Iron » PDB 2bmo-2c1v » 2bu9
Atomistry »
  Iron »
    PDB 2bmo-2c1v »
      2bu9 »

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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy