Atomistry » Iron » PDB 1m6z-1mko » 1mhl
Atomistry »
  Iron »
    PDB 1m6z-1mko »
      1mhl »

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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy