Iron in PDB 1dhy: KKS102 Bphc Enzyme

All present enzymatic activity of KKS102 Bphc Enzyme:
1.13.11.39;

The structure of KKS102 Bphc Enzyme, PDB code: 1dhy was solved by T.Senda, K.Sugiyama, H.Narita, Y.Mitsui, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	123.000, 123.000, 110.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 24.6

The binding sites of Iron atom in the KKS102 Bphc Enzyme (pdb code 1dhy). 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 KKS102 Bphc Enzyme, PDB code: 1dhy:

Iron binding site 1 out of 1 in the KKS102 Bphc Enzyme


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of KKS102 Bphc Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe293 b:18.3 occ:1.00 NE2 A:HIS145 2.3 11.4 1.0 NE2 A:HIS209 2.4 14.9 1.0 OE1 A:GLU260 2.4 17.6 1.0 CE1 A:HIS209 3.2 13.5 1.0 CE1 A:HIS145 3.2 10.6 1.0 CD2 A:HIS145 3.4 11.8 1.0 CD A:GLU260 3.4 11.1 1.0 CD2 A:HIS209 3.5 13.9 1.0 OE2 A:GLU260 3.8 11.6 1.0 OH A:TYR249 3.9 9.7 1.0 NE2 A:HIS194 4.0 21.6 1.0 ND1 A:HIS209 4.4 14.5 1.0 ND1 A:HIS145 4.4 12.2 1.0 CE1 A:HIS194 4.4 14.3 1.0 CG A:HIS145 4.5 7.6 1.0 CG A:HIS209 4.5 9.2 1.0 CB A:MET211 4.5 5.2 1.0 CE1 A:HIS240 4.6 13.5 1.0 CG A:GLU260 4.7 8.7 1.0 CG2 A:VAL147 4.7 3.5 1.0 CZ A:TYR249 4.7 7.8 1.0 CE2 A:TYR249 4.8 4.5 1.0 CB A:GLU260 4.8 2.0 1.0 CG A:MET211 4.9 8.1 1.0

T.Senda, K.Sugiyama, H.Narita, T.Yamamoto, K.Kimbara, M.Fukuda, M.Sato, K.Yano, Y.Mitsui. Three-Dimensional Structures of Free Form and Two Substrate Complexes of An Extradiol Ring-Cleavage Type Dioxygenase, the Bphc Enzyme From Pseudomonas Sp. Strain KKS102. J.Mol.Biol. V. 255 735 1996.
ISSN: ISSN 0022-2836
PubMed: 8636975
DOI: 10.1006/JMBI.1996.0060