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Iron in PDB 3a8g: Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile

Enzymatic activity of Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile

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

Protein crystallography data

The structure of Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile, PDB code: 3a8g 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) 19.01 / 1.11
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.411, 60.268, 81.810, 90.00, 124.92, 90.00
R / Rfree (%) 14.2 / 16.9

Other elements in 3a8g:

The structure of Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile (pdb code 3a8g). 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 Trimethylacetonitrile, PDB code: 3a8g:

Iron binding site 1 out of 1 in 3a8g

Go back to Iron Binding Sites List in 3a8g
Iron binding site 1 out of 1 in the Crystal Structure of Nitrile Hydratase Mutant S113A Complexed with Trimethylacetonitrile


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 Trimethylacetonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:6.3
occ:1.00
 N A:CSO114 2.0 7.3 1.0
N A:NO207 2.0 9.5 1.0
N A:ALA113 2.0 6.5 1.0
SG A:CSD112 2.2 7.0 1.0
SG A:CSO114 2.2 9.2 1.0
SG A:CYS109 2.3 7.2 1.0
C A:ALA113 2.8 7.2 1.0
CA A:ALA113 2.9 7.4 1.0
CA A:CSO114 3.0 7.8 1.0
O A:NO207 3.0 26.7 1.0
CB A:CSO114 3.0 8.8 1.0
OD1 A:CSD112 3.1 8.1 1.0
C A:CSD112 3.1 6.5 1.0
OD A:CSO114 3.1 11.6 1.0
OD2 A:CSD112 3.1 7.3 1.0
CB A:CSD112 3.1 6.9 1.0
CB A:CYS109 3.3 7.2 1.0
CA A:CSD112 3.5 6.9 1.0
N A:CSD112 3.9 6.8 1.0
CB A:ALA113 4.0 9.7 1.0
O A:ALA113 4.0 7.4 1.0
O A:CSD112 4.2 7.3 1.0
C A:CSO114 4.3 7.3 1.0
CA A:CYS109 4.7 7.1 1.0
O A:CSO114 4.7 8.1 1.0
NH2 B:ARG141 4.8 8.6 1.0
O A:HOH239 4.9 12.6 1.0
C A:LEU111 4.9 6.7 1.0
O A:CYS109 4.9 7.4 1.0
O A:THR162 5.0 11.7 1.0

Reference:

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
Page generated: Sun Aug 4 06:44:26 2024

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