1YWA

0.9 A Structure of NP4 from Rhodnius Prolixus complexed with CO 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	9
Details	BINDING SITE FOR RESIDUE PO4 A 187

Chain	Residue
A	ASP27
A	ALA144
A	ALA145
A	SER165
A	LYS167
A	HOH318
A	HOH322
A	HOH408
A	HOH409

---

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 A 188

Chain	Residue
A	THR10
A	GLY11
A	PRO37
A	LYS38
A	ARG39
A	HOH278
A	HOH296

---

site_id	AC3
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 185

Chain	Residue
A	VAL25
A	TYR28
A	VAL36
A	TYR40
A	LEU44
A	LEU57
A	HIS59
A	PHE68
A	ASP70
A	PHE86
A	LYS88
A	TYR105
A	PHE107
A	LEU123
A	LYS125
A	LYS128
A	LEU130
A	LEU133
A	CMO186
A	HOH283
A	HOH384
A	HOH452
A	HOH495
A	HOH543
A	HOH544

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CMO A 186

Chain	Residue
A	LEU133
A	HEM185

---

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

---