3O26

The structure of salutaridine reductase from Papaver somniferum.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0009820	biological_process	alkaloid metabolic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0047037	molecular_function	salutaridine reductase (NADPH) activity
A	0050661	molecular_function	NADP binding
A	0097295	biological_process	morphine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NDP A 312

Chain	Residue
A	GLY19
A	ASN98
A	ALA99
A	GLY100
A	VAL101
A	ILE151
A	VAL178
A	SER179
A	TYR236
A	LYS240
A	PRO264
A	ASN21
A	GLY265
A	LEU266
A	VAL267
A	THR269
A	MET271
A	ASN272
A	HOH314
A	HOH317
A	HOH324
A	HOH326
A	LYS22
A	HOH333
A	HOH343
A	HOH362
A	HOH428
A	HOH571
A	HOH572
A	GLY23
A	ILE24
A	ARG44
A	LEU69
A	ASP70
A	VAL71

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000269|PubMed:21169353

Chain	Residue	Details
A	TYR236

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:21169353, ECO:0007744|PDB:3O26

Chain	Residue	Details
A	ASN21
A	ARG44
A	ASP70
A	ASN98
A	TYR236
A	LYS240
A	VAL267

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21169353

Chain	Residue	Details
A	TYR129
A	SER180

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