4EJ4

Structure of the delta opioid receptor bound to naltrindole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0030430	cellular_component	host cell cytoplasm
A	0031640	biological_process	killing of cells of another organism
A	0042742	biological_process	defense response to bacterium
A	0044659	biological_process	viral release from host cell by cytolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EJ4 A 500

Chain	Residue
A	ASP128
A	TYR129
A	MET132
A	VAL217
A	TRP274
A	ILE277
A	VAL281
A	ILE304
A	TYR308

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Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLTMMSVDRYIaV

Chain	Residue	Details
A	THR134-VAL150

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	27
Details	TRANSMEM: Helical; Name=1

Chain	Residue	Details
A	LEU48-VAL75

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site_id	SWS_FT_FI2
Number of Residues	27
Details	TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:22596164

Chain	Residue	Details
A	ARG76-ASN85
A	ASP145-ALA163

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site_id	SWS_FT_FI3
Number of Residues	24
Details	TRANSMEM: Helical; Name=2

Chain	Residue	Details
A	ILE86-LEU110

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site_id	SWS_FT_FI4
Number of Residues	44
Details	TOPO_DOM: Extracellular => ECO:0000269|PubMed:22596164

Chain	Residue	Details
A	MET111-LYS122
A	ALA187-SER206
A	THR285-ALA299

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site_id	SWS_FT_FI5
Number of Residues	21
Details	TRANSMEM: Helical; Name=3

Chain	Residue	Details
A	ALA123-VAL144

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site_id	SWS_FT_FI6
Number of Residues	22
Details	TRANSMEM: Helical; Name=4

Chain	Residue	Details
A	LYS164-MET186

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site_id	SWS_FT_FI7
Number of Residues	31
Details	TRANSMEM: Helical; Name=5

Chain	Residue	Details
A	TRP207-LEU238

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site_id	SWS_FT_FI8
Number of Residues	22
Details	TRANSMEM: Helical; Name=6

Chain	Residue	Details
A	MET262-TRP284

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site_id	SWS_FT_FI9
Number of Residues	21
Details	TRANSMEM: Helical; Name=7

Chain	Residue	Details
A	LEU300-LEU321

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site_id	SWS_FT_FI10
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000255

Chain	Residue	Details
A	CYS333

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site_id	SWS_FT_FI11
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	GLU1011

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site_id	SWS_FT_FI12
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	ASN1020

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site_id	SWS_FT_FI13
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:8266098

Chain	Residue	Details
A	LEU1032
A	PHE1104

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site_id	SWS_FT_FI14
Number of Residues	2
Details	BINDING: BINDING => ECO:0000303|PubMed:7831309

Chain	Residue	Details
A	SER1117
A	ASN1132

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASN1020	covalent catalysis

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