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Iron in PDB 1mhl: Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C

Enzymatic activity of Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C

All present enzymatic activity of Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C:
1.11.1.7;

Protein crystallography data

The structure of Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C, PDB code: 1mhl was solved by R.E.Fenna, J.Zeng, C.Davey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 111.700, 64.600, 94.200, 90.00, 97.90, 90.00
R / Rfree (%) 16 / n/a

Other elements in 1mhl:

The structure of Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C (pdb code 1mhl). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C, PDB code: 1mhl:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1mhl

Go back to Iron Binding Sites List in 1mhl
Iron binding site 1 out of 2 in the Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C


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 Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe605

b:14.7
occ:1.00
 FE A:HEM605 0.0 14.7 1.0
ND A:HEM605 2.0 10.6 1.0
NB A:HEM605 2.0 11.7 1.0
NC A:HEM605 2.0 8.6 1.0
NA A:HEM605 2.0 10.2 1.0
NE2 C:HIS336 2.2 5.4 1.0
C1D A:HEM605 3.0 8.2 1.0
C4C A:HEM605 3.0 7.1 1.0
C1B A:HEM605 3.0 11.2 1.0
O A:HOH647 3.0 22.6 1.0
C1C A:HEM605 3.0 8.2 1.0
C4B A:HEM605 3.0 10.3 1.0
C4A A:HEM605 3.0 10.2 1.0
C4D A:HEM605 3.1 13.1 1.0
CE1 C:HIS336 3.1 6.3 1.0
C1A A:HEM605 3.1 10.3 1.0
CD2 C:HIS336 3.2 8.6 1.0
CHD A:HEM605 3.3 5.7 1.0
CHB A:HEM605 3.4 11.1 1.0
CHC A:HEM605 3.4 8.5 1.0
CHA A:HEM605 3.5 12.2 1.0
C3C A:HEM605 4.2 9.3 1.0
C2D A:HEM605 4.2 10.6 1.0
C2C A:HEM605 4.2 7.0 1.0
C2B A:HEM605 4.3 10.5 1.0
C3D A:HEM605 4.3 10.9 1.0
C3B A:HEM605 4.3 13.2 1.0
ND1 C:HIS336 4.3 9.1 1.0
C3A A:HEM605 4.3 10.7 1.0
C2A A:HEM605 4.3 10.3 1.0
CG C:HIS336 4.3 6.7 1.0
O C:HOH579 4.7 29.0 1.0
CD2 C:LEU417 4.8 7.2 1.0
O A:HOH646 4.9 30.0 1.0
NE2 A:GLN91 5.0 7.2 1.0

Iron binding site 2 out of 2 in 1mhl

Go back to Iron Binding Sites List in 1mhl
Iron binding site 2 out of 2 in the Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Human Myeloperoxidase Isoform C Crystallized in Space Group P2(1) at pH 5.5 and 20 Deg C within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe605

b:17.9
occ:1.00
 FE B:HEM605 0.0 17.9 1.0
ND B:HEM605 1.9 10.0 1.0
NA B:HEM605 1.9 7.0 1.0
NC B:HEM605 2.1 8.8 1.0
NE2 D:HIS336 2.1 19.3 1.0
NB B:HEM605 2.1 7.8 1.0
C4D B:HEM605 2.9 10.8 1.0
CE1 D:HIS336 2.9 19.3 1.0
C1A B:HEM605 2.9 10.2 1.0
C1D B:HEM605 3.0 10.7 1.0
C4C B:HEM605 3.0 8.8 1.0
C4A B:HEM605 3.0 8.2 1.0
C1C B:HEM605 3.1 8.2 1.0
O B:HOH650 3.1 16.0 1.0
C4B B:HEM605 3.1 7.7 1.0
C1B B:HEM605 3.1 11.6 1.0
CD2 D:HIS336 3.1 15.5 1.0
CHA B:HEM605 3.3 10.8 1.0
CHD B:HEM605 3.4 9.8 1.0
CHC B:HEM605 3.4 7.6 1.0
CHB B:HEM605 3.5 10.1 1.0
ND1 D:HIS336 4.1 17.8 1.0
C3D B:HEM605 4.1 10.2 1.0
C2D B:HEM605 4.2 9.0 1.0
C2A B:HEM605 4.2 9.4 1.0
CG D:HIS336 4.2 17.6 1.0
C3C B:HEM605 4.2 6.4 1.0
C3A B:HEM605 4.2 5.8 1.0
C2C B:HEM605 4.3 6.6 1.0
C3B B:HEM605 4.3 11.0 1.0
C2B B:HEM605 4.3 9.9 1.0
CD2 D:LEU417 4.7 11.5 1.0
O B:HOH649 4.8 21.2 1.0
O D:HOH580 5.0 28.8 1.0

Reference:

R.Fenna, J.Zeng, C.Davey. Structure of the Green Heme in Myeloperoxidase. Arch.Biochem.Biophys. V. 316 653 1995.
ISSN: ISSN 0003-9861
PubMed: 7840679
DOI: 10.1006/ABBI.1995.1086
Page generated: Sat Aug 3 10:41:19 2024

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