Iron in PDB 2ve1: Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR)

All present enzymatic activity of Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR):
1.21.3.1;

The structure of Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR), PDB code: 2ve1 was solved by W.Ge, I.J.Clifton, 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)	60.75 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.672, 75.717, 101.910, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 24.6

The binding sites of Iron atom in the Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR) (pdb code 2ve1). 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 with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR), PDB code: 2ve1:

Iron binding site 1 out of 1 in the Isopenicillin N Synthase with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR)


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 with Substrate Analogue Asmcov (Oxygen Exposed 1MIN 20BAR) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:6.2 occ:1.00 OD1 A:ASP216 2.0 4.2 1.0 O A:HOH555 2.2 6.2 1.0 NE2 A:HIS270 2.2 2.8 1.0 NE2 A:HIS214 2.3 3.4 1.0 O31 A:W2X402 2.3 18.4 0.5 S17 A:M11403 2.4 19.8 0.5 S17 A:W2X402 2.5 6.0 0.5 C33 A:M11403 2.7 13.7 0.5 CG A:ASP216 3.1 3.9 1.0 CD2 A:HIS214 3.2 3.6 1.0 CD2 A:HIS270 3.2 2.9 1.0 CE1 A:HIS270 3.2 3.2 1.0 CE1 A:HIS214 3.3 3.6 1.0 C37 A:W2X402 3.4 19.5 0.5 C32 A:W2X402 3.4 20.1 0.5 C32 A:M11403 3.5 25.2 0.5 OD2 A:ASP216 3.5 5.0 1.0 C33 A:W2X402 3.6 21.9 0.5 C16 A:W2X402 3.7 13.3 0.5 CAV A:M11403 3.9 26.4 0.5 C25 A:W2X402 4.1 13.3 0.5 C25 A:M11403 4.2 27.8 0.5 ND1 A:HIS270 4.3 3.0 1.0 CG A:HIS270 4.3 3.0 1.0 CG A:HIS214 4.3 3.9 1.0 ND1 A:HIS214 4.4 3.9 1.0 C37 A:M11403 4.4 24.9 0.5 CB A:ASP216 4.4 3.6 1.0 O29 A:M11403 4.4 25.4 0.5 C30 A:M11403 4.6 24.6 0.5 CA A:ASP216 4.7 3.2 1.0 C13 A:M11403 4.8 25.2 0.5 C30 A:W2X402 4.9 18.7 0.5 C12 A:W2X402 4.9 12.9 0.5 C12 A:M11403 4.9 23.7 0.5 N A:ASP216 4.9 4.6 1.0 O A:HOH610 4.9 16.9 1.0

W.Ge, I.J.Clifton, A.R.Howard-Jones, J.E.Stok, R.M.Adlington, J.E.Baldwin, P.J.Rutledge. Structural Studies on the Reaction of Isopenicillin N Synthase with A Sterically Demanding Depsipeptide Substrate Analogue. Chembiochem V. 10 2025 2009.
ISSN: ISSN 1439-4227
PubMed: 19598184
DOI: 10.1002/CBIC.200900080