Atomistry » Iron » PDB 3a0g-3ae5 » 3a8m
Atomistry »
  Iron »
    PDB 3a0g-3ae5 »
      3a8m »

Iron in PDB 3a8m: Crystal Structure of Nitrile Hydratase Mutant Y72F Complexed with Trimethylacetonitrile

Enzymatic activity of Crystal Structure of Nitrile Hydratase Mutant Y72F Complexed with Trimethylacetonitrile

All present enzymatic activity of Crystal Structure of Nitrile Hydratase Mutant Y72F Complexed with Trimethylacetonitrile:
4.2.1.84;

Protein crystallography data

The structure of Crystal Structure of Nitrile Hydratase Mutant Y72F Complexed with Trimethylacetonitrile, PDB code: 3a8m 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) 25.00 / 1.32
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 114.280, 60.110, 81.811, 90.00, 125.06, 90.00
R / Rfree (%) 15.7 / 19

Other elements in 3a8m:

The structure of Crystal Structure of Nitrile Hydratase Mutant Y72F 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 Y72F Complexed with Trimethylacetonitrile (pdb code 3a8m). 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 Y72F Complexed with Trimethylacetonitrile, PDB code: 3a8m:

Iron binding site 1 out of 1 in 3a8m

Go back to Iron Binding Sites List in 3a8m
Iron binding site 1 out of 1 in the Crystal Structure of Nitrile Hydratase Mutant Y72F 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 Y72F Complexed with Trimethylacetonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe300

b:5.3
occ:1.00
 O A:HOH290 2.0 10.6 1.0
N A:CSD114 2.0 4.8 1.0
N A:SER113 2.0 5.6 1.0
SG A:CSD112 2.2 6.0 1.0
SG A:CSD114 2.2 6.7 1.0
SG A:CYS109 2.3 6.2 1.0
C A:SER113 2.8 5.6 1.0
CA A:SER113 2.9 6.7 1.0
CA A:CSD114 3.0 5.4 1.0
OD1 A:CSD112 3.0 7.0 1.0
C A:CSD112 3.1 5.5 1.0
CB A:CSD114 3.1 7.2 1.0
OD2 A:CSD114 3.1 7.8 1.0
CB A:CSD112 3.1 6.5 1.0
OD2 A:CSD112 3.1 6.8 1.0
OD1 A:CSD114 3.2 8.3 1.0
CB A:CYS109 3.3 6.0 1.0
CA A:CSD112 3.5 5.1 1.0
OG A:SER113 3.7 14.1 1.0
N A:CSD112 3.9 5.3 1.0
CB A:SER113 3.9 8.1 1.0
O A:SER113 4.0 6.3 1.0
O A:CSD112 4.2 6.2 1.0
C A:CSD114 4.3 5.7 1.0
O A:CSD114 4.7 7.2 1.0
CA A:CYS109 4.7 5.7 1.0
O A:CYS109 4.9 6.8 1.0
NH2 B:ARG141 4.9 7.0 1.0
C A:LEU111 4.9 5.5 1.0
O A:HOH232 5.0 11.1 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 06:44:52 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy