Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6J79

Fusion protein of heme oxygenase-1 and NADPH-cytochrome P450 reductase (13aa)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003958	molecular_function	NADPH-hemoprotein reductase activity
A	0004128	molecular_function	cytochrome-b5 reductase activity, acting on NAD(P)H
A	0004392	molecular_function	heme oxygenase (decyclizing) activity
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005829	cellular_component	cytosol
A	0006788	biological_process	heme oxidation
A	0006809	biological_process	nitric oxide biosynthetic process
A	0007584	biological_process	response to nutrient
A	0008047	molecular_function	enzyme activator activity
A	0008941	molecular_function	nitric oxide dioxygenase NAD(P)H activity
A	0009055	molecular_function	electron transfer activity
A	0009410	biological_process	response to xenobiotic stimulus
A	0009437	biological_process	carnitine metabolic process
A	0009725	biological_process	response to hormone
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016787	molecular_function	hydrolase activity
A	0018393	biological_process	internal peptidyl-lysine acetylation
A	0019395	biological_process	fatty acid oxidation
A	0019899	molecular_function	enzyme binding
A	0022900	biological_process	electron transport chain
A	0032332	biological_process	positive regulation of chondrocyte differentiation
A	0043066	biological_process	negative regulation of apoptotic process
A	0043602	biological_process	nitrate catabolic process
A	0045880	biological_process	positive regulation of smoothened signaling pathway
A	0046210	biological_process	nitric oxide catabolic process
A	0047726	molecular_function	iron-cytochrome-c reductase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0060192	biological_process	negative regulation of lipase activity
A	0061913	biological_process	positive regulation of growth plate cartilage chondrocyte proliferation
A	0070988	biological_process	demethylation
A	0071371	biological_process	cellular response to gonadotropin stimulus
A	0071372	biological_process	cellular response to follicle-stimulating hormone stimulus
A	0071375	biological_process	cellular response to peptide hormone stimulus
A	0071548	biological_process	response to dexamethasone
A	0090031	biological_process	positive regulation of steroid hormone biosynthetic process
A	0090346	biological_process	organofluorine metabolic process
B	0003958	molecular_function	NADPH-hemoprotein reductase activity
B	0004128	molecular_function	cytochrome-b5 reductase activity, acting on NAD(P)H
B	0004392	molecular_function	heme oxygenase (decyclizing) activity
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0005829	cellular_component	cytosol
B	0006788	biological_process	heme oxidation
B	0006809	biological_process	nitric oxide biosynthetic process
B	0007584	biological_process	response to nutrient
B	0008047	molecular_function	enzyme activator activity
B	0008941	molecular_function	nitric oxide dioxygenase NAD(P)H activity
B	0009055	molecular_function	electron transfer activity
B	0009410	biological_process	response to xenobiotic stimulus
B	0009437	biological_process	carnitine metabolic process
B	0009725	biological_process	response to hormone
B	0010181	molecular_function	FMN binding
B	0016491	molecular_function	oxidoreductase activity
B	0016787	molecular_function	hydrolase activity
B	0018393	biological_process	internal peptidyl-lysine acetylation
B	0019395	biological_process	fatty acid oxidation
B	0019899	molecular_function	enzyme binding
B	0022900	biological_process	electron transport chain
B	0032332	biological_process	positive regulation of chondrocyte differentiation
B	0043066	biological_process	negative regulation of apoptotic process
B	0043602	biological_process	nitrate catabolic process
B	0045880	biological_process	positive regulation of smoothened signaling pathway
B	0046210	biological_process	nitric oxide catabolic process
B	0047726	molecular_function	iron-cytochrome-c reductase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050661	molecular_function	NADP binding
B	0060192	biological_process	negative regulation of lipase activity
B	0061913	biological_process	positive regulation of growth plate cartilage chondrocyte proliferation
B	0070988	biological_process	demethylation
B	0071371	biological_process	cellular response to gonadotropin stimulus
B	0071372	biological_process	cellular response to follicle-stimulating hormone stimulus
B	0071375	biological_process	cellular response to peptide hormone stimulus
B	0071548	biological_process	response to dexamethasone
B	0090031	biological_process	positive regulation of steroid hormone biosynthetic process
B	0090346	biological_process	organofluorine metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue FAD A 901

Chain	Residue
A	HIS492
A	VAL649
A	TYR651
A	GLY661
A	VAL662
A	ALA663
A	THR664
A	TRP850
A	ARG597
A	ARG627
A	TYR628
A	TYR629
A	SER630
A	CYS645
A	ALA646
A	VAL647

site_id	AC2
Number of Residues	18
Details	binding site for residue FMN A 902

Chain	Residue
A	SER263
A	GLN264
A	THR265
A	THR267
A	ALA268
A	ALA315
A	THR316
A	TYR317
A	GLY318
A	GLY320
A	LEU350
A	GLY351
A	ASN352
A	TYR355
A	HIS357
A	ASN359
A	ASP385
A	LEU389

site_id	AC3
Number of Residues	16
Details	binding site for residue HEM A 903

Chain	Residue
A	LYS18
A	HIS25
A	GLU29
A	MET34
A	TYR134
A	THR135
A	ARG136
A	LEU138
A	GLY139
A	SER142
A	LYS179
A	ARG183
A	PHE207
A	ASN210
A	PHE214
A	HOH1001

site_id	AC4
Number of Residues	16
Details	binding site for residue FAD B 901

Chain	Residue
B	HIS492
B	ARG597
B	ARG627
B	TYR628
B	TYR629
B	SER630
B	CYS645
B	ALA646
B	VAL647
B	TYR651
B	GLY661
B	VAL662
B	ALA663
B	THR664
B	TRP850
B	HOH1003

site_id	AC5
Number of Residues	18
Details	binding site for residue FMN B 902

Chain	Residue
B	SER263
B	GLN264
B	THR265
B	THR267
B	ALA268
B	ALA315
B	THR316
B	TYR317
B	GLY318
B	LEU350
B	GLY351
B	ASN352
B	TYR355
B	HIS357
B	PHE358
B	ASN359
B	ASP385
B	LEU389

site_id	AC6
Number of Residues	16
Details	binding site for residue HEM B 903

Chain	Residue
B	HOH1001
B	LYS18
B	HIS25
B	GLU29
B	GLN38
B	TYR134
B	THR135
B	ARG136
B	LEU138
B	GLY139
B	SER142
B	LYS179
B	ARG183
B	PHE207
B	ASN210
B	PHE214

Functional Information from PROSITE/UniProt

site_id	PS00593
Number of Residues	11
Details	HEME_OXYGENASE Heme oxygenase signature. LVAHAYTRYLG

Chain	Residue	Details
A	LEU129-GLY139

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	288
Details	Domain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	62
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P09601","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P09601","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Site: {"description":"Important for catalytic activity","evidences":[{"source":"UniProtKB","id":"P09601","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 117

Chain	Residue	Details
A	SER630	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
A	CYS803	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
A	ASP848	hydrogen bond acceptor, modifies pKa
A	TRP850	steric role

site_id	MCSA2
Number of Residues	4
Details	M-CSA 117

Chain	Residue	Details
B	SER630	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
B	CYS803	electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
B	ASP848	hydrogen bond acceptor, modifies pKa
B	TRP850	steric role

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)