Iron in PDB 3p9r: Structure of I274G Variant of E. Coli Kate

All present enzymatic activity of Structure of I274G Variant of E. Coli Kate:
1.11.1.6;

The structure of Structure of I274G Variant of E. Coli Kate, PDB code: 3p9r was solved by P.C.Loewen, V.Jha, S.Louis, P.Chelikani, X.Carpena, I.Fita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.24 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.410, 133.180, 122.740, 90.00, 109.21, 90.00
R / Rfree (%)	13.3 / 18.4

The binding sites of Iron atom in the Structure of I274G Variant of E. Coli Kate (pdb code 3p9r). 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 I274G Variant of E. Coli Kate, PDB code: 3p9r:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of I274G 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 I274G Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe760 b:10.1 occ:1.00 FE A:HDD760 0.0 10.1 1.0 OH A:TYR415 2.0 11.2 1.0 NA A:HDD760 2.0 6.4 1.0 NB A:HDD760 2.0 11.0 1.0 NC A:HDD760 2.0 11.5 1.0 ND A:HDD760 2.2 10.7 1.0 O A:HOH2520 2.8 27.0 1.0 CZ A:TYR415 3.0 9.9 1.0 C1A A:HDD760 3.0 7.6 1.0 C4C A:HDD760 3.0 9.6 1.0 C4B A:HDD760 3.1 9.8 1.0 C4A A:HDD760 3.1 8.0 1.0 C1C A:HDD760 3.1 9.7 1.0 C1B A:HDD760 3.1 11.2 1.0 C1D A:HDD760 3.1 12.5 1.0 C4D A:HDD760 3.2 10.4 1.0 CHA A:HDD760 3.4 9.0 1.0 CHC A:HDD760 3.4 13.3 1.0 CHB A:HDD760 3.4 7.8 1.0 CHD A:HDD760 3.4 10.3 1.0 CE1 A:TYR415 3.6 8.3 1.0 CE2 A:TYR415 4.0 8.5 1.0 NE A:ARG411 4.1 13.6 1.0 NH2 A:ARG411 4.2 11.1 1.0 C3C A:HDD760 4.3 6.1 1.0 C2A A:HDD760 4.3 5.8 1.0 C3A A:HDD760 4.3 5.8 1.0 C3B A:HDD760 4.3 12.4 1.0 C2C A:HDD760 4.3 11.1 1.0 C2B A:HDD760 4.3 14.1 1.0 O A:HOH1078 4.4 22.2 1.0 C2D A:HDD760 4.4 13.1 1.0 C3D A:HDD760 4.5 10.1 1.0 CZ A:ARG411 4.6 15.6 1.0 NE2 A:HIS128 4.6 10.1 1.0 CZ A:PHE214 4.6 7.8 1.0 CG2 A:VAL127 4.7 7.1 1.0 CD2 A:HIS128 4.7 7.2 1.0 CD1 A:TYR415 4.9 9.1 1.0

Iron binding site 2 out of 4 in the Structure of I274G 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 I274G Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe760 b:10.5 occ:1.00 FE B:HDD760 0.0 10.5 1.0 OH B:TYR415 1.9 8.0 1.0 NC B:HDD760 2.0 10.8 1.0 NA B:HDD760 2.0 8.8 1.0 NB B:HDD760 2.1 13.2 1.0 ND B:HDD760 2.1 7.4 1.0 O B:HOH2694 2.4 24.8 1.0 CZ B:TYR415 2.9 9.4 1.0 C4C B:HDD760 3.0 8.2 1.0 C1C B:HDD760 3.0 11.7 1.0 C4A B:HDD760 3.1 9.5 1.0 C1B B:HDD760 3.1 12.0 1.0 C1A B:HDD760 3.1 7.8 1.0 C4B B:HDD760 3.1 13.2 1.0 C4D B:HDD760 3.1 11.0 1.0 C1D B:HDD760 3.1 13.8 1.0 CHB B:HDD760 3.4 10.7 1.0 CHC B:HDD760 3.4 11.6 1.0 CHA B:HDD760 3.4 9.2 1.0 CHD B:HDD760 3.5 11.0 1.0 CE1 B:TYR415 3.6 7.4 1.0 CE2 B:TYR415 3.8 10.4 1.0 O B:HOH840 4.2 23.7 1.0 NE B:ARG411 4.2 9.4 1.0 NH2 B:ARG411 4.2 9.5 1.0 C3C B:HDD760 4.2 11.6 1.0 C2C B:HDD760 4.3 12.7 1.0 C3B B:HDD760 4.3 14.5 1.0 C3A B:HDD760 4.3 5.6 1.0 C2B B:HDD760 4.3 12.5 1.0 C2A B:HDD760 4.3 8.0 1.0 C2D B:HDD760 4.4 15.0 1.0 C3D B:HDD760 4.4 15.1 1.0 CZ B:ARG411 4.6 13.3 1.0 NE2 B:HIS128 4.6 10.4 1.0 CZ B:PHE214 4.7 9.0 1.0 CD2 B:HIS128 4.7 5.5 1.0 CG2 B:VAL127 4.7 7.2 1.0 CD1 B:TYR415 4.9 8.0 1.0

Iron binding site 3 out of 4 in the Structure of I274G 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 I274G Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe760 b:10.5 occ:1.00 FE C:HDD760 0.0 10.5 1.0 OH C:TYR415 1.9 11.8 1.0 NC C:HDD760 2.0 8.6 1.0 NB C:HDD760 2.1 14.0 1.0 NA C:HDD760 2.1 8.6 1.0 ND C:HDD760 2.2 8.9 1.0 O C:HOH2594 2.7 26.0 1.0 CZ C:TYR415 2.9 10.3 1.0 C4C C:HDD760 3.0 6.9 1.0 C1C C:HDD760 3.0 11.9 1.0 C4A C:HDD760 3.1 9.7 1.0 C4B C:HDD760 3.1 14.0 1.0 C1A C:HDD760 3.1 10.1 1.0 C1B C:HDD760 3.1 13.3 1.0 C1D C:HDD760 3.1 9.4 1.0 C4D C:HDD760 3.2 8.5 1.0 CHD C:HDD760 3.4 6.6 1.0 CHB C:HDD760 3.4 12.4 1.0 CHC C:HDD760 3.4 12.1 1.0 CHA C:HDD760 3.5 8.3 1.0 CE1 C:TYR415 3.6 9.7 1.0 CE2 C:TYR415 3.9 11.5 1.0 O C:HOH1263 4.1 23.1 1.0 NE C:ARG411 4.2 9.4 1.0 NH2 C:ARG411 4.2 9.0 1.0 C3C C:HDD760 4.2 10.8 1.0 C2C C:HDD760 4.3 7.4 1.0 C3B C:HDD760 4.3 14.5 1.0 C3A C:HDD760 4.3 8.8 1.0 C2B C:HDD760 4.3 16.6 1.0 C2A C:HDD760 4.3 8.4 1.0 C2D C:HDD760 4.4 11.2 1.0 C3D C:HDD760 4.4 10.6 1.0 CZ C:PHE214 4.6 6.0 1.0 CZ C:ARG411 4.6 11.5 1.0 NE2 C:HIS128 4.7 9.2 1.0 CG2 C:VAL127 4.7 7.0 1.0 CD2 C:HIS128 4.8 6.4 1.0 CD1 C:TYR415 4.9 7.9 1.0

Iron binding site 4 out of 4 in the Structure of I274G 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 I274G Variant of E. Coli Kate within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe760 b:9.3 occ:1.00 FE D:HDD760 0.0 9.3 1.0 NC D:HDD760 2.0 6.7 1.0 OH D:TYR415 2.0 8.6 1.0 NB D:HDD760 2.1 13.4 1.0 NA D:HDD760 2.1 5.3 1.0 ND D:HDD760 2.2 8.4 1.0 C1C D:HDD760 3.0 9.0 1.0 O D:HOH3200 3.0 32.7 1.0 C4C D:HDD760 3.0 7.6 1.0 C1A D:HDD760 3.1 4.2 1.0 CZ D:TYR415 3.1 10.6 1.0 C4B D:HDD760 3.1 14.5 1.0 C4A D:HDD760 3.1 7.6 1.0 C1B D:HDD760 3.1 13.6 1.0 C4D D:HDD760 3.2 9.7 1.0 C1D D:HDD760 3.2 11.6 1.0 CHC D:HDD760 3.4 13.6 1.0 CHA D:HDD760 3.4 6.5 1.0 CHD D:HDD760 3.5 9.2 1.0 CHB D:HDD760 3.5 9.8 1.0 CE1 D:TYR415 3.7 8.2 1.0 CE2 D:TYR415 4.0 9.8 1.0 NH2 D:ARG411 4.1 6.2 1.0 NE D:ARG411 4.2 10.7 1.0 C2C D:HDD760 4.2 9.2 1.0 C3C D:HDD760 4.2 10.8 1.0 C3B D:HDD760 4.3 13.4 1.0 C2A D:HDD760 4.3 5.5 1.0 C3A D:HDD760 4.3 3.5 1.0 C2B D:HDD760 4.3 15.2 1.0 C2D D:HDD760 4.4 10.8 1.0 C3D D:HDD760 4.4 10.7 1.0 O D:HOH1264 4.5 25.4 1.0 CZ D:ARG411 4.5 9.1 1.0 NE2 D:HIS128 4.6 10.2 1.0 CZ D:PHE214 4.6 4.1 1.0 CG2 D:VAL127 4.7 6.1 1.0 CD2 D:HIS128 4.8 3.8 1.0 CD1 D:TYR415 5.0 5.6 1.0

V.Jha, S.Louis, P.Chelikani, X.Carpena, L.J.Donald, I.Fita, P.C.Loewen. Modulation of Heme Orientation and Binding By A Single Residue in Catalase Hpii of Escherichia Coli. Biochemistry V. 50 2101 2011.
ISSN: ISSN 0006-2960
PubMed: 21332158
DOI: 10.1021/BI200027V