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Iron in PDB 1odm: Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- Vinylglycine Fe Complex)

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

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

Protein crystallography data

The structure of Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- Vinylglycine Fe Complex), PDB code: 1odm was solved by J.M.Elkins, P.J.Rutledge, N.I.Burzlaff, I.J.Clifton, R.M.Adlington, P.L.Roach, J.E.Baldwin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.00 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.701, 71.393, 100.906, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 15.2

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- Vinylglycine Fe Complex) (pdb code 1odm). 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- Vinylglycine Fe Complex), PDB code: 1odm:

Iron binding site 1 out of 1 in 1odm

Go back to Iron Binding Sites List in 1odm
Iron binding site 1 out of 1 in the Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- Vinylglycine 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- Vinylglycine Fe Complex) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1336

b:6.0
occ:1.00
 OD1 A:ASP216 2.2 6.5 1.0
O A:HOH2434 2.2 7.1 1.0
NE2 A:HIS214 2.2 6.2 1.0
NE2 A:HIS270 2.2 6.1 1.0
O A:HOH2427 2.3 6.9 1.0
S17 A:ASV1332 2.4 8.3 1.0
CE1 A:HIS270 3.1 6.4 1.0
CE1 A:HIS214 3.1 5.6 1.0
CG A:ASP216 3.2 6.3 1.0
CD2 A:HIS214 3.2 5.8 1.0
CD2 A:HIS270 3.2 6.1 1.0
C16 A:ASV1332 3.4 7.6 1.0
OD2 A:ASP216 3.5 6.7 1.0
O A:HOH2207 3.9 19.4 1.0
C33 A:ASV1332 4.1 12.7 1.0
ND1 A:HIS270 4.3 6.5 1.0
ND1 A:HIS214 4.3 6.0 1.0
CG A:HIS270 4.3 6.4 1.0
O A:HOH2485 4.3 10.9 1.0
CG A:HIS214 4.3 6.0 1.0
N29 A:ASV1332 4.4 12.9 1.0
CB A:ASP216 4.5 6.0 1.0
C12 A:ASV1332 4.7 9.7 1.0
C32 A:ASV1332 4.7 14.5 1.0
CA A:ASP216 4.8 5.9 1.0
C13 A:ASV1332 4.8 11.3 1.0
O A:HOH2435 4.9 8.4 1.0
N A:ASP216 5.0 6.0 1.0

Reference:

J.M.Elkins, P.J.Rutledge, N.I.Burzlaff, I.J.Clifton, R.M.Adlington, P.L.Roach, J.E.Baldwin. Crystallographic Studies on the Reaction of Isopenicillin N Synthase with An Unsaturated Substrate Analogue Org.Biomol.Chem. V. 1 1455 2003.
ISSN: ISSN 1477-0520
PubMed: 12926272
DOI: 10.1039/B212270G
Page generated: Sat Aug 3 12:19:10 2024

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