Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4DKL

Crystal structure of the mu-opioid receptor bound to a morphinan antagonist

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0003824	molecular_function	catalytic 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	0016787	molecular_function	hydrolase activity
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	13
Details	BINDING SITE FOR RESIDUE BF0 A 601

Chain	Residue
A	ASP147
A	TRP318
A	ILE322
A	TYR326
A	HOH718
A	TYR148
A	MET151
A	GLU229
A	LYS233
A	VAL236
A	TRP293
A	ILE296
A	VAL300

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 602

Chain	Residue
A	THR101
A	ALA102
A	THR103
A	ARG179
A	ILE278
A	HOH701
A	HOH712

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 603

Chain	Residue
A	ASN137
A	LYS141
A	THR207
A	ARG1119

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 604

Chain	Residue
A	HIS171
A	PRO172
A	VAL173
A	LYS174
A	GLY1012
A	LEU1013

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 605

Chain	Residue
A	ARG1014
A	LEU1015
A	LYS1016

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 606

Chain	Residue
A	HIS223
A	PRO224
A	THR225
A	TRP226

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 607

Chain	Residue
A	HIS223
A	HOH714
A	HOH722
A	GLY1113
A	PHE1114
A	THR1115
A	ASN1116
A	SER1117
A	ASN1132

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 608

Chain	Residue
A	HOH714
A	ARG1137

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 609

Chain	Residue
A	PHE204
A	ARG1119
A	GLN1123

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 610

Chain	Residue
A	ARG277
A	ARG280

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 611

Chain	Residue
A	HIS171
A	ARG258
A	ARG1008
A	LEU1013
A	LYS1060

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 612

Chain	Residue
A	THR1142
A	ASN1144
A	ARG1145

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 613

Chain	Residue
A	ARG95
A	TYR96
A	THR97

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CLR A 614

Chain	Residue
A	TYR299
A	ILE302
A	ILE308
A	SER317
A	HOH731

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MPG A 615

Chain	Residue
A	PHE108
A	ASN109
A	LYS185
A	ASN188
A	TRP192

site_id	BC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE MPG A 616

Chain	Residue
A	MET72
A	MET72
A	ALA73
A	TYR75
A	SER76
A	SER76
A	CYS79
A	LEU83
A	PRO122
A	SER125

site_id	BC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE A 617

Chain	Residue
A	TRP226
A	TRP226
A	LYS303
A	LYS303
A	LEU305
A	LEU305
A	ILE306
A	ILE306
A	THR307
A	THR307

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 618

Chain	Residue
A	SER261
A	GLU270

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. TSIfTLCTMSVDRYIaV

Chain	Residue	Details
A	THR153-VAL169

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	31
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	39
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	26
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Motif: {"description":"NPxxY; plays a role in stabilizing the activated conformation of the receptor","evidences":[{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P33535","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)