5MFA

Crystal structure of human promyeloperoxidase (proMPO)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003682	molecular_function	chromatin binding
A	0004601	molecular_function	peroxidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005764	cellular_component	lysosome
A	0006337	biological_process	nucleosome disassembly
A	0006952	biological_process	defense response
A	0006979	biological_process	response to oxidative stress
A	0008201	molecular_function	heparin binding
A	0009612	biological_process	response to mechanical stimulus
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0030141	cellular_component	secretory granule
A	0031491	molecular_function	nucleosome binding
A	0032094	biological_process	response to food
A	0032496	biological_process	response to lipopolysaccharide
A	0034374	biological_process	low-density lipoprotein particle remodeling
A	0035578	cellular_component	azurophil granule lumen
A	0042582	cellular_component	azurophil granule
A	0042742	biological_process	defense response to bacterium
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0043066	biological_process	negative regulation of apoptotic process
A	0045335	cellular_component	phagocytic vesicle
A	0046872	molecular_function	metal ion binding
A	0070062	cellular_component	extracellular exosome
A	0070943	biological_process	neutrophil-mediated killing of symbiont cell
A	0070944	biological_process	neutrophil-mediated killing of bacterium
A	0070947	biological_process	neutrophil-mediated killing of fungus
A	0097013	cellular_component	phagocytic vesicle lumen
A	0098869	biological_process	cellular oxidant detoxification
A	0140644	cellular_component	neutrophil extracellular trap
A	0140645	biological_process	neutrophil extracellular trap formation
A	0140776	molecular_function	protein-containing complex destabilizing activity
A	1990268	biological_process	response to gold nanoparticle

Functional Information from PROSITE/UniProt

site_id	PS00435
Number of Residues	11
Details	PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL

Chain	Residue	Details
A	GLU408-LEU418

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10766826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11705390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MHL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI10
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000220","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI11
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 601

Chain	Residue	Details
A	HIS261	proton shuttle (general acid/base)
A	MET409	electrostatic stabiliser

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