7ORC

Human Aldehyde Oxidase in complex with Raloxifene

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002138	biological_process	retinoic acid biosynthetic process
A	0004031	molecular_function	aldehyde oxidase activity
A	0004732	molecular_function	pyridoxal oxidase activity
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006805	biological_process	xenobiotic metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016623	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, oxygen as acceptor
A	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
A	0016727	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, oxygen as acceptor
A	0018488	molecular_function	aryl-aldehyde oxidase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043546	molecular_function	molybdopterin cofactor binding
A	0045429	biological_process	positive regulation of nitric oxide biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0051287	molecular_function	NAD binding
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
A	0070062	cellular_component	extracellular exosome
A	0071949	molecular_function	FAD binding
B	0002138	biological_process	retinoic acid biosynthetic process
B	0004031	molecular_function	aldehyde oxidase activity
B	0004732	molecular_function	pyridoxal oxidase activity
B	0005506	molecular_function	iron ion binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006805	biological_process	xenobiotic metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016623	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, oxygen as acceptor
B	0016661	molecular_function	oxidoreductase activity, acting on other nitrogenous compounds as donors
B	0016727	molecular_function	oxidoreductase activity, acting on CH or CH2 groups, oxygen as acceptor
B	0018488	molecular_function	aryl-aldehyde oxidase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043546	molecular_function	molybdopterin cofactor binding
B	0045429	biological_process	positive regulation of nitric oxide biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051287	molecular_function	NAD binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0070062	cellular_component	extracellular exosome
B	0071949	molecular_function	FAD binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	174
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	370
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor; for azaheterocycle hydroxylase activity","evidences":[{"source":"UniProtKB","id":"O54754","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	46
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26842593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5EPG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26842593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EPG","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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