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Iron in PDB 2ivj: Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex)

Enzymatic activity of Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex)

All present enzymatic activity of Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex):
1.21.3.1;

Protein crystallography data

The structure of Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex), PDB code: 2ivj was solved by A.R.Howard-Jones, J.M.Elkins, I.J.Clifton, P.L.Roach, R.M.Adlington, J.E.Baldwin, P.J.Rutledge, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.12 / 1.46
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.663, 71.182, 100.877, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 16.7

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex) (pdb code 2ivj). 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 From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex), PDB code: 2ivj:

Iron binding site 1 out of 1 in 2ivj

Go back to Iron Binding Sites List in 2ivj
Iron binding site 1 out of 1 in the Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex)


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 From Aspergillus Nidulans (Anaerobic Ac-Cyclopropylglycine Fe Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1335

b:8.4
occ:1.00
 OD1 A:ASP216 2.1 8.3 1.0
O A:HOH2324 2.2 10.8 1.0
NE2 A:HIS214 2.2 8.1 1.0
NE2 A:HIS270 2.2 8.3 1.0
O A:HOH2318 2.3 10.0 1.0
S17 A:BCV1332 2.4 11.3 1.0
CG A:ASP216 3.1 8.9 1.0
CE1 A:HIS270 3.1 8.3 1.0
CE1 A:HIS214 3.2 8.7 1.0
CD2 A:HIS214 3.2 7.2 1.0
CD2 A:HIS270 3.2 7.7 1.0
C16 A:BCV1332 3.4 13.2 1.0
OD2 A:ASP216 3.4 9.1 1.0
O A:HOH2143 3.9 21.3 1.0
C33 A:BCV1332 4.1 19.1 1.0
ND1 A:HIS270 4.3 7.9 1.0
ND1 A:HIS214 4.3 8.7 1.0
CG A:HIS214 4.3 7.0 1.0
CG A:HIS270 4.3 7.9 1.0
O A:HOH2363 4.4 15.9 1.0
CB A:ASP216 4.4 8.2 1.0
C32 A:BCV1332 4.7 20.7 1.0
C12 A:BCV1332 4.7 13.3 1.0
CA A:ASP216 4.8 8.3 1.0
O A:HOH2326 4.8 12.8 1.0
N A:ASP216 4.9 8.6 1.0
C13 A:BCV1332 4.9 15.1 1.0
N29 A:BCV1332 5.0 17.8 1.0

Reference:

A.R.Howard-Jones, J.M.Elkins, I.J.Clifton, P.L.Roach, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Interactions of Isopenicillin N Synthase with Cyclopropyl-Containing Substrate Analogues Reveal New Mechanistic Insight. Biochemistry V. 46 4755 2007.
ISSN: ISSN 0006-2960
PubMed: 17397141
DOI: 10.1021/BI062314Q
Page generated: Thu Jul 17 02:21:17 2025

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