1ERX

CRYSTAL STRUCTURE OF NITROPHORIN 4 COMPLEXED WITH NO

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0016491	molecular_function	oxidoreductase activity
A	0042311	biological_process	vasodilation
A	0046872	molecular_function	metal ion binding
A	0051381	molecular_function	histamine binding
A	0070026	molecular_function	nitric oxide binding
A	0097746	biological_process	blood vessel diameter maintenance

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEV A 185

Chain	Residue
A	VAL25
A	PHE86
A	LYS88
A	TYR105
A	PHE107
A	LEU123
A	LYS125
A	LEU130
A	LEU133
A	NO186
A	HOH291
A	TYR28
A	VAL36
A	TYR40
A	ALA42
A	LEU57
A	HIS59
A	PHE68
A	ASP70

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NO A 186

Chain	Residue
A	HIS59
A	LEU130
A	LEU133
A	HEV185

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIT A 347

Chain	Residue
A	ASN85
A	ASN85
A	ALA101
A	GLY102
A	GLY102
A	ASN103
A	TYR104
A	TYR104
A	HOH337

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"10876239","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11560480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14673714","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16171383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20524697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22334402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22976968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23474537","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9782054","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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