Structure of PDB 1myp Chain A

Receptor sequence
>1mypA (length=104) Species: 9615 (Canis lupus familiaris) [Search protein sequence]
CPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPG
VKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMFMQWGQLLDHDLDFT
PEPA
3D structure
PDB1myp X-ray crystal structure of canine myeloperoxidase at 3 A resolution.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Q91 D94 H95 D96
Catalytic site (residue number reindexed from 1) Q91 D94 H95 D96
Enzyme Commision number 1.11.2.2: myeloperoxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A M87 Q91 D94 D98 F99 T100 M87 Q91 D94 D98 F99 T100
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
Biological Process
GO:0006979 response to oxidative stress

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1myp, PDBe:1myp, PDBj:1myp
PDBsum1myp
PubMed1320128
UniProtP05164|PERM_HUMAN Myeloperoxidase (Gene Name=MPO)

[Back to BioLiP]