_EC 1.11.2.2 Myeloperoxidase. 14 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,663 PDB entries]
EC 1.11.-.- Acting on a peroxide as acceptor. [662 PDB entries]
EC 1.11.2.- With H(2)O(2) as acceptor, one oxygen atom of which is incorporat [19 PDB entries]
EC 1.11.2.2 Myeloperoxidase. [14 PDB entries]    
1cxp

Reaction: Cl(-) + H(2)O(2) + H(+) = HClO + H(2)O.
 

Cl(-)
+
H(2)O(2)
+ H(+)
= HClO
+ H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Mpo. Verdoperoxidase.
Cofactor(s): Ca(2+); Heme.
 
Ca(2+)

Heme
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments: Is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from Ec 1.11.1.10 in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl(2), chloramines, hydroxyl radical, singlet oxygen). Mpo also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 14 PDB entries in enzyme class E.C.1.11.2.2

  PDB code Protein
1cxp
Cryogenic crystal structure of human myeloperoxidase isoform
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1d2v
Crystal structure of bromide-bound human myeloperoxidase iso ph 5.5
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1d5l
Crystal structure of cyanide-bound human myeloperoxidase iso ph 5.5
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1d7w
Crystal structure of human myeloperoxidase isoform c complex cyanide and bromide at ph 4.0
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1dnu
Structural analyses of human myeloperoxidase-thiocyanate com
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1dnw
Human myeloperoxidase-cyanide-thiocyanate complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1mhl
Crystal structure of human myeloperoxidase isoform c crystal space group p2(1) at ph 5.5 and 20 deg c
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Organelle: azurophil granules. Organelle: azurophil granules
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
1myp
X-ray crystal structure of canine myeloperoxidase at 3 angst resolution
Source: Canis lupus familiaris. Dog. Organism_taxid: 9615. Organism_taxid: 9615
Chains: A, C, B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
3f9p
Crystal structure of myeloperoxidase from human leukocytes
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: leukocytes. Other_details: purified from human leukocytes. Other_details: purified from human leukocytes
Chains: A, C, B, D (107 residues) CATH domain: Unassigned
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
3zs0
Human myeloperoxidase inactivated by tx2
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: hl-60. Atcc: ccl240. Atcc: ccl240
Chains: A, B, C, D (104 residues) CATH domain: Unassigned
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
3zs1
Human myeloperoxidase inactivated by tx5
Source: Homo sapiens. Human. Cell_line: hl-60. Atcc: ccl240. Atcc: ccl240
Chains: A, B, C, D (104 residues) CATH domain: Unassigned
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
4c1m
Myeloperoxidase in complex with the revesible inhibitor hx1
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: blood. Cell: neutrophil. Cell: neutrophil
Chains: A, B, C, D (102 residues) CATH domain: Unassigned
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
4dl1
Crystal structure of human myeloperoxidase with covalent thi analog
Source: Homo sapiens. Human. Organism_taxid: 9606. Other_details: blood. Organism_taxid: 9606
Chains: A, C, B, D, E, G, F, H, I, K, J, L, M, O, N, P (104 residues) CATH domain: Unassigned
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme
4ejx
Structure of ceruloplasmin-myeloperoxidase complex
Source: Homo sapiens. Human. Organism_taxid: 9606. Organism_taxid: 9606
Chains: B, D (104 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme cofactor Protoheme