Iron in PDB 3emr: Crystal Structure Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens

The structure of Crystal Structure Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens, PDB code: 3emr was solved by K.Reuter, A.Heine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.85
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	102.790, 102.790, 159.070, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / 22.8

The binding sites of Iron atom in the Crystal Structure Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens (pdb code 3emr). 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 Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens, PDB code: 3emr:

Iron binding site 1 out of 1 in the Crystal Structure Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of the Ectoine Hydroxylase Ectd From Salibacillus Salexigens within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe400 b:23.9 occ:1.00 NE2 A:HIS248 2.1 21.3 1.0 O A:HOH824 2.1 36.0 1.0 O A:HOH823 2.1 31.3 1.0 NE2 A:HIS146 2.1 20.7 1.0 OD1 A:ASP148 2.2 19.9 1.0 O A:HOH851 2.4 47.9 1.0 CE1 A:HIS248 2.9 20.8 1.0 CE1 A:HIS146 3.0 23.5 1.0 CG A:ASP148 3.1 20.4 1.0 CD2 A:HIS248 3.1 17.0 1.0 CD2 A:HIS146 3.2 23.4 1.0 OD2 A:ASP148 3.4 22.3 1.0 O A:HOH889 3.8 47.6 1.0 ND1 A:HIS248 4.1 19.9 1.0 ND1 A:HIS146 4.1 21.3 1.0 CG A:HIS248 4.2 18.9 1.0 CG A:HIS146 4.2 23.5 1.0 CB A:ASP148 4.5 21.4 1.0 CA A:ASP148 4.9 18.6 1.0 N A:ASP148 4.9 18.1 1.0

K.Reuter, M.Pittelkow, J.Bursy, A.Heine, T.Craan, E.Bremer. Synthesis of 5-Hydroxyectoine From Ectoine: Crystal Structure of the Non-Heme Iron(II) and 2-Oxoglutarate-Dependent Dioxygenase Ectd Plos One V. 5 10647 2010.
ISSN: ESSN 1932-6203
PubMed: 20498719
DOI: 10.1371/JOURNAL.PONE.0010647