Iron in PDB 3buj: Crystal Structure of CALO2

The structure of Crystal Structure of CALO2, PDB code: 3buj was solved by J.G.Mccoy, H.D.Johnson, S.Singh, C.A.Bingman, J.S.Thorson, G.N.Phillipsjr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	67.27 / 2.47
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.202, 71.202, 204.451, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 25.7

The binding sites of Iron atom in the Crystal Structure of CALO2 (pdb code 3buj). 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 Crystal Structure of CALO2, PDB code: 3buj:

Iron binding site 1 out of 1 in the Crystal Structure of CALO2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of CALO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe398 b:45.3 occ:1.00 FE A:HEM398 0.0 45.3 1.0 NB A:HEM398 2.1 45.2 1.0 ND A:HEM398 2.1 46.2 1.0 NA A:HEM398 2.1 45.9 1.0 NC A:HEM398 2.1 45.8 1.0 SG A:CYS343 2.3 36.7 1.0 C4B A:HEM398 3.0 45.1 1.0 C4D A:HEM398 3.1 47.8 1.0 C1D A:HEM398 3.1 47.0 1.0 C1A A:HEM398 3.1 45.4 1.0 C1C A:HEM398 3.1 45.1 1.0 C1B A:HEM398 3.1 45.9 1.0 C4C A:HEM398 3.1 46.2 1.0 C4A A:HEM398 3.1 46.2 1.0 O A:HOH483 3.3 69.6 1.0 CB A:CYS343 3.4 37.7 1.0 CHC A:HEM398 3.4 45.6 1.0 CHA A:HEM398 3.4 45.8 1.0 CHD A:HEM398 3.5 46.9 1.0 CHB A:HEM398 3.5 46.1 1.0 CA A:CYS343 4.1 37.5 1.0 C3B A:HEM398 4.3 45.6 1.0 C2B A:HEM398 4.3 45.9 1.0 C2D A:HEM398 4.3 46.9 1.0 C3D A:HEM398 4.3 48.8 1.0 C2C A:HEM398 4.3 46.1 1.0 C3C A:HEM398 4.3 46.9 1.0 C2A A:HEM398 4.3 46.8 1.0 C3A A:HEM398 4.4 46.3 1.0 N A:GLY345 4.8 36.2 1.0 C A:CYS343 4.8 37.4 1.0 N A:LEU344 4.9 37.0 1.0

J.G.Mccoy, H.D.Johnson, S.Singh, C.A.Bingman, I.K.Lei, J.S.Thorson, G.N.Phillips Jr.. Structural Characterization of CALO2: A Putative Orsellinic Acid P450 Oxidase in the Calicheamicin Biosynthetic Pathway. Proteins V. 74 50 2009.
ISSN: ISSN 0887-3585
PubMed: 18561189
DOI: 10.1002/PROT.22131