2E3B

Crystal structure of the HA-bound form of Arthromyces ramosus peroxidase at 1.3 Angstroms resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000302	biological_process	response to reactive oxygen species
A	0004601	molecular_function	peroxidase activity
A	0005576	cellular_component	extracellular region
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
A	0034599	biological_process	cellular response to oxidative stress
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
A	0140825	molecular_function	lactoperoxidase activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLU176-LEU186

---

site_id	PS00436
Number of Residues	12
Details	PEROXIDASE_2 Peroxidases active site signature. VRkiLRIvFHDA

Chain	Residue	Details
A	VAL47-ALA58

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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	9
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"description":"axial binding residue"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"1576150","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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