Iron in PDB 3ttu: Structure of F413Y/H128N Double Variant of E. Coli Kate

All present enzymatic activity of Structure of F413Y/H128N Double Variant of E. Coli Kate:
1.11.1.6;

The structure of Structure of F413Y/H128N Double Variant of E. Coli Kate, PDB code: 3ttu was solved by P.C.Loewen, V.Jha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.46 / 1.89
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.620, 132.960, 122.670, 90.00, 109.39, 90.00
R / Rfree (%)	14.4 / 19.3

The binding sites of Iron atom in the Structure of F413Y/H128N Double Variant of E. Coli Kate (pdb code 3ttu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of F413Y/H128N Double Variant of E. Coli Kate, PDB code: 3ttu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of F413Y/H128N Double Variant of E. Coli Kate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of F413Y/H128N Double Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe760 b:10.6 occ:1.00 FE A:HEM760 0.0 10.6 1.0 OH A:TYR415 2.0 11.7 1.0 NA A:HEM760 2.0 7.0 1.0 NC A:HEM760 2.1 8.9 1.0 NB A:HEM760 2.1 8.9 1.0 ND A:HEM760 2.1 8.3 1.0 CZ A:TYR415 3.0 10.1 1.0 C4C A:HEM760 3.1 7.3 1.0 C1A A:HEM760 3.1 8.2 1.0 C1C A:HEM760 3.1 7.8 1.0 C1B A:HEM760 3.1 7.0 1.0 C4A A:HEM760 3.1 7.3 1.0 C4B A:HEM760 3.1 8.7 1.0 C4D A:HEM760 3.1 9.1 1.0 C1D A:HEM760 3.1 7.8 1.0 O A:HOH3246 3.4 13.6 1.0 CHD A:HEM760 3.4 9.1 1.0 CHC A:HEM760 3.5 10.2 1.0 CHB A:HEM760 3.5 7.2 1.0 CHA A:HEM760 3.5 7.8 1.0 CE1 A:TYR415 3.6 10.2 1.0 CE2 A:TYR415 3.9 9.1 1.0 NE A:ARG411 4.1 7.2 1.0 NH2 A:ARG411 4.2 4.0 1.0 C3C A:HEM760 4.3 7.2 1.0 C2B A:HEM760 4.3 7.7 1.0 C3B A:HEM760 4.3 8.2 1.0 C3A A:HEM760 4.3 7.5 1.0 C2C A:HEM760 4.3 9.0 1.0 C2A A:HEM760 4.3 9.5 1.0 C2D A:HEM760 4.3 6.7 1.0 O A:HOH3213 4.3 13.7 1.0 C3D A:HEM760 4.3 7.5 1.0 CZ A:ARG411 4.5 9.0 1.0 CG2 A:VAL127 4.6 7.4 1.0 CZ A:PHE214 4.7 7.0 1.0 CD1 A:TYR415 4.9 8.5 1.0

Iron binding site 2 out of 4 in the Structure of F413Y/H128N Double Variant of E. Coli Kate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of F413Y/H128N Double Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe760 b:11.1 occ:1.00 FE B:HEM760 0.0 11.1 1.0 OH B:TYR415 1.9 13.1 1.0 NA B:HEM760 2.0 8.5 1.0 ND B:HEM760 2.1 9.2 1.0 NC B:HEM760 2.1 8.6 1.0 NB B:HEM760 2.1 10.8 1.0 CZ B:TYR415 2.9 10.7 1.0 C4D B:HEM760 3.0 12.1 1.0 C4C B:HEM760 3.1 8.9 1.0 C1A B:HEM760 3.1 9.9 1.0 C4A B:HEM760 3.1 11.2 1.0 C4B B:HEM760 3.1 10.2 1.0 C1D B:HEM760 3.1 10.3 1.0 C1C B:HEM760 3.1 7.5 1.0 C1B B:HEM760 3.1 9.0 1.0 CHD B:HEM760 3.4 8.8 1.0 CHC B:HEM760 3.4 10.4 1.0 CHA B:HEM760 3.4 8.7 1.0 O B:HOH3263 3.4 15.6 1.0 CHB B:HEM760 3.5 7.5 1.0 CE1 B:TYR415 3.5 7.5 1.0 CE2 B:TYR415 3.8 10.1 1.0 NE B:ARG411 4.1 8.6 1.0 NH2 B:ARG411 4.2 6.7 1.0 C3C B:HEM760 4.3 8.0 1.0 C3D B:HEM760 4.3 11.1 1.0 C2A B:HEM760 4.3 9.2 1.0 C3A B:HEM760 4.3 7.5 1.0 C2C B:HEM760 4.3 8.2 1.0 C2D B:HEM760 4.3 9.5 1.0 C2B B:HEM760 4.3 10.2 1.0 C3B B:HEM760 4.3 9.6 1.0 O B:HOH3262 4.4 15.8 1.0 CZ B:ARG411 4.6 9.3 1.0 CG2 B:VAL127 4.6 8.6 1.0 CZ B:PHE214 4.8 10.4 1.0 CD1 B:TYR415 4.9 9.4 1.0

Iron binding site 3 out of 4 in the Structure of F413Y/H128N Double Variant of E. Coli Kate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of F413Y/H128N Double Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe760 b:11.4 occ:1.00 FE C:HEM760 0.0 11.4 1.0 OH C:TYR415 1.9 13.5 1.0 ND C:HEM760 2.1 7.4 1.0 NA C:HEM760 2.1 9.3 1.0 NB C:HEM760 2.1 12.5 1.0 NC C:HEM760 2.1 8.4 1.0 CZ C:TYR415 2.9 8.8 1.0 C4B C:HEM760 3.1 9.0 1.0 C4D C:HEM760 3.1 7.3 1.0 C4A C:HEM760 3.1 9.6 1.0 C1D C:HEM760 3.1 9.7 1.0 C1B C:HEM760 3.1 10.0 1.0 C4C C:HEM760 3.1 5.7 1.0 C1A C:HEM760 3.1 9.7 1.0 C1C C:HEM760 3.2 11.9 1.0 O C:HOH3247 3.3 14.2 1.0 CHD C:HEM760 3.5 8.7 1.0 CHB C:HEM760 3.5 9.6 1.0 CHC C:HEM760 3.5 10.2 1.0 CHA C:HEM760 3.5 9.3 1.0 CE1 C:TYR415 3.6 8.5 1.0 CE2 C:TYR415 3.9 10.6 1.0 NE C:ARG411 4.0 7.6 1.0 NH2 C:ARG411 4.1 7.2 1.0 C3B C:HEM760 4.3 9.2 1.0 C2B C:HEM760 4.3 10.1 1.0 C3D C:HEM760 4.3 6.7 1.0 C3A C:HEM760 4.3 9.4 1.0 C2D C:HEM760 4.3 6.2 1.0 C2A C:HEM760 4.3 8.8 1.0 C3C C:HEM760 4.3 10.1 1.0 O C:HOH3248 4.3 16.4 1.0 C2C C:HEM760 4.4 8.4 1.0 CZ C:ARG411 4.5 10.7 1.0 CG2 C:VAL127 4.6 7.8 1.0 CZ C:PHE214 4.7 8.3 1.0 CD1 C:TYR415 4.9 9.6 1.0 CD C:ARG411 5.0 6.3 1.0

Iron binding site 4 out of 4 in the Structure of F413Y/H128N Double Variant of E. Coli Kate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of F413Y/H128N Double Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe760 b:10.7 occ:1.00 FE D:HEM760 0.0 10.7 1.0 OH D:TYR415 1.9 10.4 1.0 NC D:HEM760 2.0 7.0 1.0 NB D:HEM760 2.1 8.4 1.0 NA D:HEM760 2.1 7.9 1.0 ND D:HEM760 2.2 9.3 1.0 CZ D:TYR415 3.0 9.2 1.0 C1C D:HEM760 3.0 7.5 1.0 C4C D:HEM760 3.1 7.2 1.0 C4B D:HEM760 3.1 6.9 1.0 C1A D:HEM760 3.1 5.5 1.0 C4A D:HEM760 3.1 5.7 1.0 C4D D:HEM760 3.1 8.1 1.0 C1B D:HEM760 3.1 8.7 1.0 C1D D:HEM760 3.2 9.9 1.0 CHC D:HEM760 3.4 7.0 1.0 CHA D:HEM760 3.4 7.0 1.0 O D:HOH3243 3.5 11.6 1.0 CHB D:HEM760 3.5 6.7 1.0 CHD D:HEM760 3.5 8.7 1.0 CE1 D:TYR415 3.7 8.6 1.0 CE2 D:TYR415 3.9 10.0 1.0 NE D:ARG411 4.0 6.0 1.0 NH2 D:ARG411 4.1 5.0 1.0 C2C D:HEM760 4.3 8.3 1.0 C3C D:HEM760 4.3 10.1 1.0 C3B D:HEM760 4.3 7.4 1.0 C3A D:HEM760 4.3 7.3 1.0 O D:HOH3242 4.3 12.0 1.0 C2A D:HEM760 4.3 7.5 1.0 C2B D:HEM760 4.4 8.7 1.0 C3D D:HEM760 4.4 7.5 1.0 C2D D:HEM760 4.4 8.4 1.0 CZ D:ARG411 4.5 9.8 1.0 CG2 D:VAL127 4.6 8.2 1.0 CZ D:PHE214 4.7 7.3 1.0 CD1 D:TYR415 4.9 9.5 1.0

V.Jha, L.J.Donald, P.C.Loewen. Mutation of PHE413 to Tyr in Catalase Kate From Escherichia Coli Leads to Side Chain Damage and Main Chain Cleavage. Arch.Biochem.Biophys. V. 525 207 2012.
ISSN: ISSN 0003-9861
PubMed: 22172685
DOI: 10.1016/J.ABB.2011.11.022