Iron in PDB 6pm7: The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution

All present enzymatic activity of The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution:
1.11.1.6;

The structure of The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution, PDB code: 6pm7 was solved by A.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	121.99 / 1.85
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	140.865, 140.865, 101.840, 90.00, 90.00, 120.00
R / Rfree (%)	19.2 / 23.2

The binding sites of Iron atom in the The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution (pdb code 6pm7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution, PDB code: 6pm7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:46.4 occ:1.00 FE A:HEM601 0.0 46.4 1.0 ND A:HEM601 1.9 46.0 1.0 NA A:HEM601 2.0 48.4 1.0 OH A:TYR357 2.0 43.7 1.0 NB A:HEM601 2.1 45.3 1.0 NC A:HEM601 2.1 62.5 1.0 C1D A:HEM601 2.9 54.3 1.0 C4D A:HEM601 2.9 52.2 1.0 C1A A:HEM601 3.0 48.0 1.0 C1B A:HEM601 3.0 52.0 1.0 C4C A:HEM601 3.0 60.5 1.0 C4B A:HEM601 3.0 51.1 1.0 C4A A:HEM601 3.1 45.5 1.0 CZ A:TYR357 3.1 50.2 1.0 C1C A:HEM601 3.1 57.3 1.0 CHD A:HEM601 3.4 55.3 1.0 CHA A:HEM601 3.4 47.4 1.0 CHB A:HEM601 3.4 48.0 1.0 CHC A:HEM601 3.5 49.8 1.0 HE A:ARG353 3.6 49.0 1.0 HH21 A:ARG353 3.7 52.2 1.0 HE2 A:TYR357 3.7 43.6 1.0 O A:HOH860 3.8 65.9 1.0 CE2 A:TYR357 3.8 43.6 1.0 HZ A:PHE160 3.8 42.0 1.0 HG21 A:VAL73 3.9 55.5 1.0 CE1 A:TYR357 4.0 47.1 1.0 HE1 A:TYR357 4.0 47.1 1.0 C2D A:HEM601 4.1 54.9 1.0 C3D A:HEM601 4.2 50.8 1.0 C2A A:HEM601 4.3 46.0 1.0 C3A A:HEM601 4.3 48.3 1.0 C3C A:HEM601 4.3 70.4 1.0 C2B A:HEM601 4.3 53.8 1.0 C2C A:HEM601 4.3 63.8 1.0 C3B A:HEM601 4.3 49.5 1.0 NE A:ARG353 4.3 49.0 1.0 HHD A:HEM601 4.3 55.3 1.0 HG23 A:VAL73 4.3 55.5 1.0 HHA A:HEM601 4.3 47.4 1.0 NH2 A:ARG353 4.3 52.2 1.0 HE2 A:HIS74 4.3 50.3 1.0 CZ A:PHE160 4.3 42.0 1.0 HD2 A:HIS74 4.3 48.3 1.0 HHB A:HEM601 4.4 48.0 1.0 HHC A:HEM601 4.4 49.8 1.0 CG2 A:VAL73 4.6 55.5 1.0 NE2 A:HIS74 4.7 50.3 1.0 CZ A:ARG353 4.7 50.2 1.0 CD2 A:HIS74 4.7 48.3 1.0 HG2 A:ARG353 4.8 45.4 1.0 HE1 A:PHE160 4.8 45.4 1.0 HG22 A:VAL73 4.9 55.5 1.0 CE1 A:PHE160 4.9 45.4 1.0 HH22 A:ARG353 4.9 52.2 1.0 HG11 A:VAL145 5.0 44.0 1.0

Iron binding site 2 out of 2 in the The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of the Triclinic Crystal Form of Beef Liver Catalase at 1.85 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe601 b:44.8 occ:1.00 FE B:HEM601 0.0 44.8 1.0 OH B:TYR357 1.9 44.1 1.0 ND B:HEM601 1.9 43.3 1.0 NA B:HEM601 2.0 42.8 1.0 NB B:HEM601 2.1 47.2 1.0 NC B:HEM601 2.1 51.7 1.0 C1D B:HEM601 2.9 42.1 1.0 C4D B:HEM601 2.9 43.4 1.0 CZ B:TYR357 3.0 43.6 1.0 C1A B:HEM601 3.0 42.3 1.0 C4B B:HEM601 3.0 46.4 1.0 C4C B:HEM601 3.0 48.1 1.0 C4A B:HEM601 3.1 45.5 1.0 C1B B:HEM601 3.1 47.7 1.0 C1C B:HEM601 3.1 62.0 1.0 CHA B:HEM601 3.4 41.5 1.0 CHD B:HEM601 3.4 41.0 1.0 CHC B:HEM601 3.5 54.1 1.0 HE B:ARG353 3.5 42.6 1.0 CHB B:HEM601 3.5 51.5 1.0 HH21 B:ARG353 3.5 50.8 1.0 HE2 B:TYR357 3.6 38.3 1.0 CE2 B:TYR357 3.7 38.3 1.0 CE1 B:TYR357 3.9 41.1 1.0 HE1 B:TYR357 3.9 41.1 1.0 HZ B:PHE160 3.9 53.0 1.0 O B:HOH732 4.0 76.2 1.0 HG21 B:VAL73 4.0 49.2 1.0 C2D B:HEM601 4.2 44.2 1.0 NE B:ARG353 4.2 42.6 1.0 C3D B:HEM601 4.2 42.1 1.0 NH2 B:ARG353 4.2 50.8 1.0 C2A B:HEM601 4.2 41.3 1.0 C3A B:HEM601 4.2 43.0 1.0 C3C B:HEM601 4.3 61.0 1.0 C3B B:HEM601 4.3 44.1 1.0 C2B B:HEM601 4.3 46.2 1.0 HHA B:HEM601 4.3 41.5 1.0 C2C B:HEM601 4.3 63.5 1.0 HE2 B:HIS74 4.3 46.5 1.0 HHD B:HEM601 4.3 41.0 1.0 HD2 B:HIS74 4.3 44.5 1.0 HG23 B:VAL73 4.3 49.2 1.0 HHC B:HEM601 4.4 54.1 1.0 HHB B:HEM601 4.4 51.5 1.0 CZ B:PHE160 4.4 53.0 1.0 CZ B:ARG353 4.6 50.7 1.0 CG2 B:VAL73 4.6 49.2 1.0 NE2 B:HIS74 4.7 46.5 1.0 CD2 B:HIS74 4.8 44.5 1.0 HG2 B:ARG353 4.8 39.0 1.0 HH22 B:ARG353 4.8 50.8 1.0 HE1 B:PHE160 4.9 55.7 1.0 HG11 B:VAL145 4.9 47.2 1.0 HG22 B:VAL73 4.9 49.2 1.0 CE1 B:PHE160 5.0 55.7 1.0 HG12 B:VAL145 5.0 47.2 1.0 CD2 B:TYR357 5.0 39.6 1.0

A.Mcpherson, A.Mcpherson. N/A N/A.