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7UL4

CryoEM Structure of Inactive MOR Bound to Alvimopan and Mb6

Functional Information from GO Data
ChainGOidnamespacecontents
A0001965molecular_functionG-protein alpha-subunit binding
A0004930molecular_functionG protein-coupled receptor activity
A0004979molecular_functionbeta-endorphin receptor activity
A0004985molecular_functionG protein-coupled opioid receptor activity
A0005245molecular_functionvoltage-gated calcium channel activity
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007197biological_processadenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0007218biological_processneuropeptide signaling pathway
A0007626biological_processlocomotory behavior
A0016020cellular_componentmembrane
A0016529cellular_componentsarcoplasmic reticulum
A0019226biological_processtransmission of nerve impulse
A0019233biological_processsensory perception of pain
A0019904molecular_functionprotein domain specific binding
A0030315cellular_componentT-tubule
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031635biological_processadenylate cyclase-inhibiting opioid receptor signaling pathway
A0031681molecular_functionG-protein beta-subunit binding
A0032100biological_processpositive regulation of appetite
A0032590cellular_componentdendrite membrane
A0032839cellular_componentdendrite cytoplasm
A0033685biological_processnegative regulation of luteinizing hormone secretion
A0035176biological_processsocial behavior
A0038003biological_processG protein-coupled opioid receptor signaling pathway
A0038047molecular_functionmorphine receptor activity
A0042383cellular_componentsarcolemma
A0042713biological_processsperm ejaculation
A0042734cellular_componentpresynaptic membrane
A0042755biological_processeating behavior
A0042923molecular_functionneuropeptide binding
A0043005cellular_componentneuron projection
A0043204cellular_componentperikaryon
A0045019biological_processnegative regulation of nitric oxide biosynthetic process
A0045211cellular_componentpostsynaptic membrane
A0045471biological_processresponse to ethanol
A0045722biological_processpositive regulation of gluconeogenesis
A0048149biological_processbehavioral response to ethanol
A0050769biological_processpositive regulation of neurogenesis
A0051481biological_processnegative regulation of cytosolic calcium ion concentration
A0060079biological_processexcitatory postsynaptic potential
A0061358biological_processnegative regulation of Wnt protein secretion
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0070588biological_processcalcium ion transmembrane transport
A0071315biological_processcellular response to morphine
A0080135biological_processregulation of cellular response to stress
A0097444cellular_componentspine apparatus
A0098982cellular_componentGABA-ergic synapse
A0099171biological_processpresynaptic modulation of chemical synaptic transmission
A0106072biological_processnegative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway
A2000310biological_processregulation of NMDA receptor activity
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLCTMSVDRYIaV
ChainResidueDetails
ATHR153-VAL169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues17
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"NPxxY; plays a role in stabilizing the activated conformation of the receptor","evidences":[{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P33535","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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