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Chlorine 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:

Iron (Fe) 2 atoms
Calcium (Ca) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine 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 Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1mhl

Go back to Chlorine Binding Sites List in 1mhl
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl602

b:2.0
occ:1.00
 O A:HOH672 3.0 13.6 1.0
N A:TRP32 3.1 11.5 1.0
N C:VAL327 3.4 4.8 1.0
CH2 C:TRP436 3.7 6.2 1.0
CA A:ARG31 3.7 14.6 1.0
CB C:ASN326 3.7 7.4 1.0
C A:ARG31 3.8 12.2 1.0
CB C:VAL327 3.9 7.2 1.0
N C:ASN326 3.9 7.8 1.0
CG1 C:VAL327 4.0 4.6 1.0
CZ2 C:TRP436 4.1 9.1 1.0
N A:LEU33 4.1 11.5 1.0
CA A:TRP32 4.1 9.8 1.0
O A:VAL30 4.1 10.8 1.0
CA C:ASN326 4.1 5.1 1.0
CB A:TRP32 4.2 11.6 1.0
C C:ASN326 4.2 6.3 1.0
CD2 C:LEU430 4.2 4.5 1.0
CA C:VAL327 4.3 7.1 1.0
CD A:ARG31 4.4 18.3 1.0
CB A:ARG31 4.4 17.2 1.0
O A:LEU33 4.5 13.5 1.0
CB C:ALA325 4.5 5.0 1.0
C A:TRP32 4.6 13.8 1.0
C C:ALA325 4.7 7.2 1.0
NH1 A:ARG31 4.7 11.3 1.0
N A:ARG31 4.8 13.8 1.0
CZ3 C:TRP436 4.8 10.5 1.0
CG A:ARG31 4.9 21.4 1.0
C A:VAL30 4.9 12.1 1.0
CG A:TRP32 4.9 10.7 1.0
CG C:ASN326 4.9 8.4 1.0
O A:ARG31 5.0 9.9 1.0

Chlorine binding site 2 out of 2 in 1mhl

Go back to Chlorine Binding Sites List in 1mhl
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl602

b:2.0
occ:1.00
 N B:TRP32 3.0 13.3 1.0
O B:HOH677 3.2 13.5 1.0
N D:VAL327 3.4 11.2 1.0
CA B:ARG31 3.5 13.0 1.0
C B:ARG31 3.7 12.1 1.0
N D:ASN326 3.7 8.0 1.0
CH2 D:TRP436 3.8 9.7 1.0
CB D:ASN326 3.8 8.1 1.0
CB D:VAL327 3.8 10.9 1.0
CG1 D:VAL327 3.9 4.4 1.0
O B:VAL30 4.1 11.6 1.0
CA D:ASN326 4.1 10.7 1.0
CA B:TRP32 4.1 11.3 1.0
CB B:ARG31 4.1 13.9 1.0
CZ2 D:TRP436 4.2 9.7 1.0
C D:ASN326 4.2 11.5 1.0
N B:LEU33 4.2 8.7 1.0
CB B:TRP32 4.2 11.9 1.0
CA D:VAL327 4.2 11.7 1.0
CG B:ARG31 4.3 14.9 1.0
CD2 D:LEU430 4.4 4.5 1.0
CB D:ALA325 4.5 2.2 1.0
C D:ALA325 4.5 7.5 1.0
O B:LEU33 4.6 10.7 1.0
C B:TRP32 4.6 11.3 1.0
N B:ARG31 4.7 12.2 1.0
CG B:TRP32 4.8 17.2 1.0
CD B:ARG31 4.8 18.8 1.0
C B:VAL30 4.9 10.4 1.0
CA D:ALA325 4.9 6.7 1.0
CZ3 D:TRP436 4.9 8.9 1.0
O B:ARG31 4.9 11.4 1.0
NH1 B:ARG31 4.9 12.3 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: Thu Jul 10 18:13:59 2025

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