Iron in PDB 5kik: Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State

The structure of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State, PDB code: 5kik was solved by C.J.Knoot, J.D.Lipscomb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.88 / 2.20
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	153.529, 153.529, 93.043, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 21.3

The structure of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State (pdb code 5kik). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State, PDB code: 5kik:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:45.9 occ:1.00 O A:HOH776 1.9 43.7 1.0 ND1 A:HIS307 2.1 42.0 1.0 OE1 A:GLU377 2.2 44.7 1.0 OE2 A:GLU377 2.2 44.2 1.0 NE2 A:HIS305 2.3 41.8 1.0 OD2 A:ASP403 2.4 43.7 1.0 CD A:GLU377 2.6 44.8 1.0 CE1 A:HIS307 3.0 42.1 1.0 CD2 A:HIS305 3.1 42.5 1.0 CG A:HIS307 3.2 38.7 1.0 CE1 A:HIS305 3.3 41.4 1.0 FE A:FE602 3.3 52.1 1.0 CG A:ASP403 3.4 56.8 1.0 CB A:HIS307 3.6 41.3 1.0 CB A:ASP403 3.8 50.8 1.0 CG A:GLU377 4.1 46.1 1.0 NE2 A:HIS310 4.1 47.7 1.0 NE2 A:HIS307 4.2 42.8 1.0 CD2 A:HIS310 4.2 45.7 1.0 CD2 A:HIS307 4.3 40.5 1.0 O A:HOH865 4.3 51.1 1.0 CG A:HIS305 4.3 40.0 1.0 ND1 A:HIS305 4.4 46.6 1.0 OD1 A:ASP309 4.5 46.1 1.0 OD1 A:ASP403 4.6 51.2 1.0 O A:GLU377 5.0 39.8 1.0 CB A:GLU377 5.0 43.9 1.0

Iron binding site 2 out of 2 in the Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cmla Beta-Hydroxylase in Chemically Reduced Diferrous State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:52.1 occ:1.00 O A:HOH776 2.1 43.7 1.0 OD2 A:ASP403 2.2 43.7 1.0 O A:HOH865 2.2 51.1 1.0 OD2 A:ASP309 2.3 51.7 1.0 NE2 A:HIS310 2.3 47.7 1.0 O A:HOH740 2.3 48.4 1.0 CD2 A:HIS310 3.1 45.7 1.0 CG A:ASP309 3.1 48.8 1.0 CG A:ASP403 3.1 56.8 1.0 OD1 A:ASP309 3.3 46.1 1.0 FE A:FE601 3.3 45.9 1.0 OD1 A:ASP403 3.3 51.2 1.0 CE1 A:HIS310 3.4 54.8 1.0 NE2 A:HIS258 4.0 51.7 1.0 OE1 A:GLU377 4.1 44.7 1.0 O A:HOH791 4.2 63.2 1.0 NE2 A:HIS305 4.3 41.8 1.0 CG A:HIS310 4.3 48.3 1.0 ND1 A:HIS310 4.4 48.5 1.0 CE1 A:HIS305 4.4 41.4 1.0 CB A:ASP309 4.5 48.2 1.0 CB A:ASP403 4.5 50.8 1.0 CE1 A:HIS258 4.8 54.4 1.0 O A:ALA482 5.0 55.5 1.0 ND1 A:HIS307 5.0 42.0 1.0

A.J.Jasniewski, C.J.Knoot, J.D.Lipscomb, L.Que. A Carboxylate Shift Regulates Dioxygen Activation By the Diiron Nonheme Beta-Hydroxylase Cmla Upon Binding of A Substrate-Loaded Nonribosomal Peptide Synthetase. Biochemistry V. 55 5818 2016.
ISSN: ISSN 1520-4995
PubMed: 27668828
DOI: 10.1021/ACS.BIOCHEM.6B00834