Iron in PDB 6jqq: Kate H392C From Escherichia Coli

All present enzymatic activity of Kate H392C From Escherichia Coli:
1.11.1.6;

The structure of Kate H392C From Escherichia Coli, PDB code: 6jqq was solved by J.B.Park, H.-S.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.16 / 2.40
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	90.345, 129.099, 117.372, 90.00, 109.86, 90.00
R / Rfree (%)	24.4 / 27.9

The binding sites of Iron atom in the Kate H392C From Escherichia Coli (pdb code 6jqq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Kate H392C From Escherichia Coli, PDB code: 6jqq:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Kate H392C From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Kate H392C From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:29.5 occ:1.00 FE A:HEM801 0.0 29.5 1.0 OH A:TYR415 1.9 29.1 1.0 ND A:HEM801 1.9 29.5 1.0 NA A:HEM801 2.0 28.8 1.0 NC A:HEM801 2.0 29.4 1.0 NB A:HEM801 2.1 28.9 1.0 CZ A:TYR415 2.8 28.3 1.0 C4D A:HEM801 2.9 28.6 1.0 C1D A:HEM801 2.9 29.1 1.0 C1A A:HEM801 2.9 28.4 1.0 C4C A:HEM801 3.0 28.7 1.0 C1B A:HEM801 3.0 29.0 1.0 C4B A:HEM801 3.0 30.0 1.0 C4A A:HEM801 3.0 28.2 1.0 C1C A:HEM801 3.0 29.9 1.0 CHA A:HEM801 3.3 29.0 1.0 CHD A:HEM801 3.4 28.3 1.0 CHB A:HEM801 3.4 28.3 1.0 CHC A:HEM801 3.4 29.9 1.0 CE2 A:TYR415 3.5 28.8 1.0 CE1 A:TYR415 3.8 28.7 1.0 C2A A:HEM801 4.1 27.2 1.0 C2D A:HEM801 4.2 29.0 1.0 C3D A:HEM801 4.2 29.1 1.0 NE A:ARG411 4.2 26.4 1.0 C2C A:HEM801 4.2 29.9 1.0 C3A A:HEM801 4.2 27.6 1.0 C3C A:HEM801 4.2 29.2 1.0 NH2 A:ARG411 4.2 25.2 1.0 C2B A:HEM801 4.2 29.4 1.0 C3B A:HEM801 4.3 30.0 1.0 CZ A:ARG411 4.5 25.7 1.0 CG2 A:VAL127 4.5 26.6 1.0 CD2 A:HIS128 4.7 24.4 1.0 NE2 A:HIS128 4.7 24.6 1.0 CZ A:PHE214 4.7 25.8 1.0 CD2 A:TYR415 4.8 28.9 1.0 CD1 A:TYR415 5.0 29.0 1.0

Iron binding site 2 out of 4 in the Kate H392C From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Kate H392C From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:36.5 occ:1.00 FE B:HEM801 0.0 36.5 1.0 OH B:TYR415 1.2 33.6 1.0 ND B:HEM801 1.9 34.0 1.0 NA B:HEM801 2.0 33.3 1.0 NC B:HEM801 2.1 33.2 1.0 NB B:HEM801 2.1 34.4 1.0 CZ B:TYR415 2.4 31.5 1.0 C1D B:HEM801 2.9 33.2 1.0 C4D B:HEM801 2.9 33.2 1.0 C1A B:HEM801 2.9 32.5 1.0 C4C B:HEM801 3.0 32.5 1.0 C4B B:HEM801 3.0 34.2 1.0 C4A B:HEM801 3.0 32.6 1.0 C1B B:HEM801 3.1 34.6 1.0 C1C B:HEM801 3.1 33.9 1.0 CE2 B:TYR415 3.3 31.4 1.0 CE1 B:TYR415 3.3 32.4 1.0 CHD B:HEM801 3.3 33.4 1.0 CHA B:HEM801 3.3 33.0 1.0 CHB B:HEM801 3.5 33.7 1.0 CHC B:HEM801 3.5 34.0 1.0 C2D B:HEM801 4.1 33.0 1.0 C2A B:HEM801 4.1 32.4 1.0 C3D B:HEM801 4.1 33.3 1.0 C3C B:HEM801 4.2 33.5 1.0 C3A B:HEM801 4.2 32.2 1.0 NH2 B:ARG411 4.2 29.2 1.0 C2C B:HEM801 4.2 33.1 1.0 C2B B:HEM801 4.3 33.7 1.0 C3B B:HEM801 4.3 33.9 1.0 NE B:ARG411 4.4 28.9 1.0 CG2 B:VAL127 4.4 25.6 1.0 NE2 B:HIS128 4.5 27.9 1.0 CZ B:PHE214 4.5 26.0 1.0 CD2 B:HIS128 4.5 27.4 1.0 CD2 B:TYR415 4.6 30.0 1.0 CD1 B:TYR415 4.6 30.4 1.0 CZ B:ARG411 4.7 28.9 1.0

Iron binding site 3 out of 4 in the Kate H392C From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Kate H392C From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe801 b:27.5 occ:1.00 FE C:HEM801 0.0 27.5 1.0 ND C:HEM801 1.9 26.9 1.0 OH C:TYR415 1.9 27.3 1.0 NA C:HEM801 2.0 26.7 1.0 NC C:HEM801 2.1 26.0 1.0 NB C:HEM801 2.1 25.8 1.0 C4D C:HEM801 2.8 27.0 1.0 C1D C:HEM801 2.9 26.6 1.0 C1A C:HEM801 2.9 26.7 1.0 CZ C:TYR415 2.9 27.3 1.0 C4C C:HEM801 3.0 25.5 1.0 C4A C:HEM801 3.0 26.8 1.0 C1B C:HEM801 3.0 25.9 1.0 C4B C:HEM801 3.0 25.9 1.0 C1C C:HEM801 3.1 25.9 1.0 CHA C:HEM801 3.3 27.1 1.0 CHD C:HEM801 3.3 25.5 1.0 CHB C:HEM801 3.4 26.6 1.0 CHC C:HEM801 3.5 25.8 1.0 CE2 C:TYR415 3.7 27.2 1.0 CE1 C:TYR415 3.8 27.8 1.0 C3D C:HEM801 4.1 26.9 1.0 C2D C:HEM801 4.1 27.0 1.0 C2A C:HEM801 4.1 26.8 1.0 C3A C:HEM801 4.2 26.1 1.0 C3C C:HEM801 4.2 25.8 1.0 NE C:ARG411 4.2 26.4 1.0 C2C C:HEM801 4.2 26.0 1.0 C2B C:HEM801 4.3 26.1 1.0 C3B C:HEM801 4.3 24.9 1.0 NH2 C:ARG411 4.4 25.5 1.0 CG2 C:VAL127 4.5 24.8 1.0 CZ C:PHE214 4.6 22.5 1.0 NE2 C:HIS128 4.6 22.7 1.0 CD2 C:HIS128 4.7 23.6 1.0 CZ C:ARG411 4.7 25.6 1.0 CD2 C:TYR415 5.0 26.9 1.0 CE2 C:PHE214 5.0 23.2 1.0

Iron binding site 4 out of 4 in the Kate H392C From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Kate H392C From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:32.5 occ:1.00 FE D:HEM801 0.0 32.5 1.0 ND D:HEM801 1.9 31.3 1.0 OH D:TYR415 2.0 28.6 1.0 NA D:HEM801 2.0 30.4 1.0 NC D:HEM801 2.1 30.7 1.0 NB D:HEM801 2.1 30.3 1.0 C1D D:HEM801 2.9 31.4 1.0 C4D D:HEM801 2.9 31.4 1.0 CZ D:TYR415 2.9 29.0 1.0 C1A D:HEM801 2.9 30.1 1.0 C4C D:HEM801 3.0 30.3 1.0 C4A D:HEM801 3.0 29.9 1.0 C1B D:HEM801 3.0 30.3 1.0 C4B D:HEM801 3.0 31.2 1.0 C1C D:HEM801 3.1 30.5 1.0 CHD D:HEM801 3.3 31.8 1.0 CHA D:HEM801 3.3 31.3 1.0 CHB D:HEM801 3.4 30.4 1.0 CHC D:HEM801 3.5 30.9 1.0 CE2 D:TYR415 3.5 29.1 1.0 CE1 D:TYR415 3.9 29.9 1.0 C2D D:HEM801 4.1 30.7 1.0 NH2 D:ARG411 4.1 30.2 1.0 C3D D:HEM801 4.1 31.0 1.0 C2A D:HEM801 4.1 29.2 1.0 C3A D:HEM801 4.2 29.7 1.0 C3C D:HEM801 4.2 30.5 1.0 NE D:ARG411 4.2 29.1 1.0 C2B D:HEM801 4.2 30.3 1.0 C3B D:HEM801 4.3 30.9 1.0 C2C D:HEM801 4.3 29.7 1.0 CG2 D:VAL127 4.6 25.5 1.0 CZ D:PHE214 4.6 24.9 1.0 NE2 D:HIS128 4.6 24.2 1.0 CZ D:ARG411 4.6 29.2 1.0 CD2 D:HIS128 4.7 24.3 1.0 CD2 D:TYR415 4.8 28.5 1.0

J.B.Park, H.-S.Cho. Kate H392C From Escherichia Coli To Be Published.