Iron in PDB 3a8h: Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide

All present enzymatic activity of Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide:
4.2.1.84;

The structure of Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide, PDB code: 3a8h was solved by Y.Yamanaka, K.Hashimoto, A.Ohtaki, K.Noguchi, M.Yohda, M.Odaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.09 / 1.66
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	113.606, 60.012, 81.499, 90.00, 125.14, 90.00
R / Rfree (%)	17.3 / 20

The binding sites of Iron atom in the Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide (pdb code 3a8h). 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 Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide, PDB code: 3a8h:

Iron binding site 1 out of 1 in the Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide


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 Nitrile Hydratase Mutant S113A Complexed with Trimethylacetamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:11.2 occ:1.00 N A:CSO114 2.0 9.7 1.0 N A:ALA113 2.1 9.7 1.0 O A:HOH502 2.1 17.4 1.0 SG A:CSD112 2.1 10.0 1.0 SG A:CSO114 2.2 14.2 1.0 SG A:CYS109 2.3 9.8 1.0 C A:ALA113 2.8 9.6 1.0 CA A:ALA113 2.9 9.4 1.0 CA A:CSO114 3.0 10.7 1.0 OD1 A:CSD112 3.1 10.8 1.0 CB A:CSO114 3.1 10.5 1.0 C A:CSD112 3.1 9.7 1.0 CB A:CSD112 3.1 10.0 1.0 OD2 A:CSD112 3.2 10.6 1.0 OD A:CSO114 3.2 16.5 1.0 CB A:CYS109 3.3 10.0 1.0 CA A:CSD112 3.4 9.9 1.0 N A:CSD112 3.9 10.0 1.0 CB A:ALA113 4.0 9.9 1.0 O A:ALA113 4.0 9.3 1.0 O A:CSD112 4.2 9.7 1.0 C A:CSO114 4.3 10.1 1.0 O A:CSO114 4.7 9.9 1.0 CA A:CYS109 4.7 9.0 1.0 NH2 B:ARG141 4.8 11.4 1.0 O A:CYS109 4.8 10.0 1.0 C A:LEU111 4.9 9.6 1.0 O A:HOH265 5.0 14.8 1.0 O A:THR162 5.0 13.3 1.0

Y.Yamanaka, K.Hashimoto, A.Ohtaki, K.Noguchi, M.Yohda, M.Odaka. Kinetic and Structural Studies on Roles of the Serine Ligand and A Strictly Conserved Tyrosine Residue in Nitrile Hydratase J.Biol.Inorg.Chem. V. 15 655 2010.
ISSN: ISSN 0949-8257
PubMed: 20221653
DOI: 10.1007/S00775-010-0632-3