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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9RKF

Dark structure of beta-2 Adrenergic receptor with photoazolol in Dark state recorded at SwissFEL

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0003824molecular_functioncatalytic activity
A0009253biological_processpeptidoglycan catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwTLCVIAVDRYFaI
ChainResidueDetails
AALA119-ILE135
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive 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"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues36
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU240proton shuttle (general acid/base)
AASP249covalent catalysis

254917

PDB entries from 2026-06-10

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