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Iron in PDB 7dmr: Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution

Enzymatic activity of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution

All present enzymatic activity of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution, PDB code: 7dmr was solved by P.K.Singh, C.Rani, P.Sharma, S.Sharma, T.P.Singh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.61 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.240, 85.310, 98.930, 90.00, 90.00, 90.00
R / Rfree (%) 19 / 24.3

Other elements in 7dmr:

The structure of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution also contains other interesting chemical elements:

Potassium (K) 1 atom
Zinc (Zn) 2 atoms
Calcium (Ca) 1 atom
Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution (pdb code 7dmr). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution, PDB code: 7dmr:

Iron binding site 1 out of 1 in 7dmr

Go back to Iron Binding Sites List in 7dmr
Iron binding site 1 out of 1 in the Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:23.2
occ:1.00
 FE A:HEM605 0.0 23.2 1.0
O A:HOH720 1.7 17.8 1.0
ND A:HEM605 1.9 23.6 1.0
NA A:HEM605 2.0 21.4 1.0
NE2 A:HIS351 2.0 25.6 1.0
NC A:HEM605 2.1 22.0 1.0
NB A:HEM605 2.1 24.2 1.0
C1D A:HEM605 2.9 23.0 1.0
C4D A:HEM605 3.0 22.3 1.0
C1A A:HEM605 3.0 21.7 1.0
CE1 A:HIS351 3.0 26.9 1.0
C4C A:HEM605 3.0 22.5 1.0
CD2 A:HIS351 3.0 24.5 1.0
C4A A:HEM605 3.1 22.5 1.0
C1C A:HEM605 3.1 22.8 1.0
C4B A:HEM605 3.1 23.8 1.0
C1B A:HEM605 3.2 22.1 1.0
CHA A:HEM605 3.3 20.9 1.0
CHD A:HEM605 3.4 24.4 1.0
CHC A:HEM605 3.5 22.6 1.0
CHB A:HEM605 3.5 21.4 1.0
K A:K609 3.6 29.2 1.0
ND1 A:HIS351 4.1 25.4 1.0
CG A:HIS351 4.1 24.1 1.0
C2A A:HEM605 4.2 22.2 1.0
C2D A:HEM605 4.2 22.1 1.0
C3A A:HEM605 4.2 21.3 1.0
C3C A:HEM605 4.2 21.0 1.0
C2C A:HEM605 4.2 21.7 1.0
C3D A:HEM605 4.3 22.2 1.0
C2B A:HEM605 4.4 23.0 1.0
NE2 A:GLN105 4.4 18.3 1.0
C3B A:HEM605 4.4 24.5 1.0
CD2 A:LEU433 4.7 19.6 1.0
O1D A:HEM605 4.9 28.9 0.5

Reference:

P.K.Singh, C.Rani, P.Sharma, S.Shrama, T.P.Singh. Crystal Structure of Potassium Induced Heme Modification in Yak Lactoperoxidase at 2.20 A Resolution To Be Published.
Page generated: Thu Aug 8 04:02:13 2024

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