Iron in PDB 5kil: Cmla Beta-Hydroxylase E377D Mutant

The structure of Cmla Beta-Hydroxylase E377D Mutant, PDB code: 5kil 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)	38.49 / 2.72
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	153.954, 153.954, 92.548, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 26.2

The structure of Cmla Beta-Hydroxylase E377D Mutant also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Cmla Beta-Hydroxylase E377D Mutant (pdb code 5kil). 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 E377D Mutant, PDB code: 5kil:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cmla Beta-Hydroxylase E377D Mutant


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 E377D Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:61.3 occ:1.00 FE1 A:FEO601 0.0 61.3 1.0 O A:FEO601 1.8 48.7 1.0 OD2 A:ASP377 1.9 70.2 1.0 ND1 A:HIS307 2.0 50.9 1.0 OD2 A:ASP403 2.1 75.1 1.0 NE2 A:HIS305 2.4 53.4 1.0 CE1 A:HIS307 2.6 49.6 1.0 CG A:ASP377 2.9 69.7 1.0 CD2 A:HIS305 3.1 60.2 1.0 CG A:ASP403 3.2 60.8 1.0 OD1 A:ASP377 3.2 73.8 1.0 CG A:HIS307 3.3 47.2 1.0 CE1 A:HIS305 3.5 58.3 1.0 FE2 A:FEO601 3.5 68.0 0.7 CB A:ASP403 3.6 52.7 1.0 NE2 A:HIS307 3.9 45.4 1.0 CB A:HIS307 3.9 50.5 1.0 O A:ACT603 4.0 74.9 0.7 CD2 A:HIS307 4.2 47.4 1.0 CB A:ASP377 4.2 55.0 1.0 OD1 A:ASP403 4.3 68.5 1.0 NE2 A:HIS310 4.3 57.9 1.0 CG A:HIS305 4.4 49.8 1.0 CD2 A:HIS310 4.4 60.6 1.0 ND1 A:HIS305 4.5 57.0 1.0 O A:ASP377 4.6 69.0 1.0 OD2 A:ASP309 4.7 63.6 1.0 C A:ACT603 4.9 74.1 0.7 OXT A:ACT603 4.9 69.0 0.7

Iron binding site 2 out of 2 in the Cmla Beta-Hydroxylase E377D Mutant


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 E377D Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:68.0 occ:0.70 FE2 A:FEO601 0.0 68.0 0.7 OD2 A:ASP309 1.8 63.6 1.0 OXT A:ACT603 2.1 69.0 0.7 O A:ACT603 2.3 74.9 0.7 O A:FEO601 2.3 48.7 1.0 NE2 A:HIS310 2.4 57.9 1.0 OD2 A:ASP403 2.5 75.1 1.0 C A:ACT603 2.5 74.1 0.7 CG A:ASP309 3.0 62.5 1.0 CD2 A:HIS310 3.0 60.6 1.0 OD1 A:ASP403 3.1 68.5 1.0 CG A:ASP403 3.1 60.8 1.0 FE1 A:FEO601 3.5 61.3 1.0 CE1 A:HIS310 3.6 53.4 1.0 OD1 A:ASP309 3.7 66.8 1.0 NE2 A:HIS258 3.7 52.4 1.0 CH3 A:ACT603 3.9 64.7 0.7 CB A:ASP309 4.0 53.9 1.0 CG A:HIS310 4.3 58.4 1.0 NE2 A:HIS305 4.3 53.4 1.0 CE1 A:HIS258 4.5 53.4 1.0 ND1 A:HIS310 4.5 48.9 1.0 CB A:ASP403 4.6 52.7 1.0 CE1 A:HIS305 4.7 58.3 1.0 ND1 A:HIS307 4.7 50.9 1.0 CD2 A:HIS258 4.7 58.9 1.0 CB A:HIS307 5.0 50.5 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