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Iron in PDB 7p3l: Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys

Enzymatic activity of Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys

All present enzymatic activity of Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys:
1.21.3.1;

Protein crystallography data

The structure of Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys, PDB code: 7p3l was solved by P.Rabe, I.Clifton, C.J.Schofield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.33 / 1.32
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.98, 71.42, 101.08, 90, 90, 90
R / Rfree (%) 15.1 / 17.3

Iron Binding Sites:

The binding sites of Iron atom in the Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys (pdb code 7p3l). 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 in Complex with Fe and the Substrate Analogue Aadcyshomocys, PDB code: 7p3l:

Iron binding site 1 out of 1 in 7p3l

Go back to Iron Binding Sites List in 7p3l
Iron binding site 1 out of 1 in the Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys


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 in Complex with Fe and the Substrate Analogue Aadcyshomocys within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:11.7
occ:1.00
O A:HOH574 2.1 14.7 1.0
NE2 A:HIS214 2.2 13.0 1.0
NE2 A:HIS270 2.2 11.7 1.0
OD1 A:ASP216 2.2 12.3 1.0
SG A:CYS408 2.4 12.8 1.0
SD A:KCY409 2.5 13.4 1.0
CE1 A:HIS214 3.2 11.7 1.0
CE1 A:HIS270 3.2 13.5 1.0
HB2 A:CYS408 3.2 14.8 1.0
CG A:ASP216 3.2 11.8 1.0
CD2 A:HIS214 3.2 11.2 1.0
CD2 A:HIS270 3.2 11.6 1.0
HE1 A:HIS214 3.3 14.0 1.0
HE1 A:HIS270 3.3 16.2 1.0
HD2 A:HIS214 3.4 13.4 1.0
HD2 A:HIS270 3.4 13.9 1.0
CB A:CYS408 3.4 12.3 1.0
OD2 A:ASP216 3.6 12.9 1.0
HGA A:KCY409 3.6 17.2 1.0
CG A:KCY409 3.6 14.4 1.0
HBA A:KCY409 3.7 16.8 1.0
HN A:KCY409 3.9 15.6 1.0
HB3 A:CYS408 3.9 14.8 1.0
CB A:KCY409 4.2 14.0 1.0
O A:HOH792 4.3 15.4 1.0
ND1 A:HIS270 4.3 12.5 1.0
HA A:ASP216 4.3 12.3 1.0
ND1 A:HIS214 4.3 11.8 1.0
N A:KCY409 4.3 13.0 1.0
CG A:HIS270 4.4 12.2 1.0
CG A:HIS214 4.4 11.5 1.0
CB A:ASP216 4.5 10.8 1.0
HG A:KCY409 4.5 17.2 1.0
CA A:CYS408 4.7 12.3 1.0
C A:CYS408 4.8 12.6 1.0
CA A:ASP216 4.8 10.3 1.0
HG21 A:THR221 4.9 14.3 1.0
CA A:KCY409 4.9 12.2 1.0
HE2 A:PHE211 4.9 17.3 1.0
HB3 A:ASP216 5.0 12.9 1.0
HD21 A:ASN252 5.0 17.7 1.0
N A:ASP216 5.0 12.5 1.0

Reference:

P.Rabe, I.Clifton, C.J.Schofield. Isopenicillin N Synthase in Complex with Fe and the Substrate Analogue Aadcyshomocys To Be Published.
Page generated: Thu Aug 8 14:55:00 2024

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