5AOG

Structure of Sorghum peroxidase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0006950	biological_process	response to stress
A	0006979	biological_process	response to oxidative stress
A	0009505	cellular_component	plant-type cell wall
A	0016491	molecular_function	oxidoreductase activity
A	0020037	molecular_function	heme binding
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. DLVALSGGHTI

Chain	Residue	Details
A	ASP203-ILE213

---

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

Chain	Residue	Details
A	ALA72-CYS83

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P22195","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26666777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26666777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26666777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P22195","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26666777","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5AOG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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