Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9ZZO

MP1104-bound Kappa Opioid Receptor in complex with beta-arrestin1

Functional Information from GO Data
ChainGOidnamespacecontents
C0000139cellular_componentGolgi membrane
C0000785cellular_componentchromatin
C0001664molecular_functionG protein-coupled receptor binding
C0001678biological_processintracellular glucose homeostasis
C0001934biological_processpositive regulation of protein phosphorylation
C0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
C0002031biological_processG protein-coupled receptor internalization
C0002092biological_processpositive regulation of receptor internalization
C0003713molecular_functiontranscription coactivator activity
C0004402molecular_functionhistone acetyltransferase activity
C0004857molecular_functionenzyme inhibitor activity
C0004869molecular_functioncysteine-type endopeptidase inhibitor activity
C0005096molecular_functionGTPase activator activity
C0005159molecular_functioninsulin-like growth factor receptor binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005765cellular_componentlysosomal membrane
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0005929cellular_componentcilium
C0006357biological_processregulation of transcription by RNA polymerase II
C0006511biological_processubiquitin-dependent protein catabolic process
C0007166biological_processcell surface receptor signaling pathway
C0007600biological_processsensory perception
C0016567biological_processprotein ubiquitination
C0019899molecular_functionenzyme binding
C0030659cellular_componentcytoplasmic vesicle membrane
C0030666cellular_componentendocytic vesicle membrane
C0030674molecular_functionprotein-macromolecule adaptor activity
C0031143cellular_componentpseudopodium
C0031410cellular_componentcytoplasmic vesicle
C0031434molecular_functionmitogen-activated protein kinase kinase binding
C0031625molecular_functionubiquitin protein ligase binding
C0031701molecular_functionangiotensin receptor binding
C0032715biological_processnegative regulation of interleukin-6 production
C0032717biological_processnegative regulation of interleukin-8 production
C0035025biological_processpositive regulation of Rho protein signal transduction
C0035721biological_processintraciliary retrograde transport
C0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
C0042981biological_processregulation of apoptotic process
C0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
C0043149biological_processstress fiber assembly
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0045746biological_processnegative regulation of Notch signaling pathway
C0045880biological_processpositive regulation of smoothened signaling pathway
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0060090molecular_functionmolecular adaptor activity
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0097499biological_processprotein localization to non-motile cilium
C1902533biological_processpositive regulation of intracellular signal transduction
C1903568biological_processnegative regulation of protein localization to ciliary membrane
C1990763molecular_functionarrestin family protein binding
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLTMMSVDRYIaV
ChainResidueDetails
ATHR144-VAL160
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR193-HIS199
HTYR204-HIS210
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
CPHE61-LEU79
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsRegion: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues38
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33742150","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DW9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"33742150","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DW9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"33742150","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DW9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"37209686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GOC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8I10","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"37209686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GOC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8I10","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues27
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues12
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails

260626

PDB entries from 2026-10-07

PDB statisticsPDBj update infoContact PDBjnumon