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

Enzymatic activity of 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;

Protein crystallography data

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

Iron Binding Sites:

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 6pm7

Go back to Iron Binding Sites List in 6pm7
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 6pm7

Go back to Iron Binding Sites List in 6pm7
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

Reference:

A.Mcpherson, A.Mcpherson. N/A N/A.
Page generated: Wed Aug 7 05:43:24 2024

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