1YWB

0.9 A Structure of NP4 from Rhodnius Prolixus complexed with NO at pH 5.6

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 187

Chain	Residue
A	THR10
A	HOH514
A	GLY11
A	PRO37
A	LYS38
A	ARG39
A	LYS63
A	HOH284
A	HOH312
A	HOH498

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 185

Chain	Residue
A	VAL36
A	TYR40
A	LEU57
A	HIS59
A	PHE68
A	ASP70
A	PHE86
A	LYS88
A	TYR105
A	LEU123
A	LYS125
A	LYS128
A	LEU130
A	LEU133
A	NO186
A	HOH292
A	HOH408
A	HOH409

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NO A 186

Chain	Residue
A	LEU123
A	LEU133
A	HEM185

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: proximal binding residue => ECO:0000269|PubMed:10876239, ECO:0000269|PubMed:11560480, ECO:0000269|PubMed:14673714, ECO:0000269|PubMed:16171383, ECO:0000269|PubMed:20524697, ECO:0000269|PubMed:22334402, ECO:0000269|PubMed:22976968, ECO:0000269|PubMed:23474537, ECO:0000269|PubMed:9782054

Chain	Residue	Details
A	HIS59

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