Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PS6

XFEL beta2 AR structure by ligand exchange from Timolol to Timolol.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0004941molecular_functionbeta2-adrenergic receptor activity
A0006940biological_processregulation of smooth muscle contraction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
A0097746biological_processblood vessel diameter maintenance
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue TIM A 1201
ChainResidue
AASP113
APHE289
APHE290
AASN293
ATYR308
AASN312
AVAL114
AVAL117
ATHR118
ATYR199
ASER203
ASER204
ASER207
ATRP286

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 1202
ChainResidue
ATHR66
AVAL67
ATHR68
AARG131
ATYR141
ASER143

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 A 1203
ChainResidue
ALYS270
ALYS273
AARG328

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 1204
ChainResidue
APHE1114
AASN1116
ASER1117
AASN1132

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 1205
ChainResidue
ATHR1142
AASN1144
AARG1145

site_idAC6
Number of Residues5
Detailsbinding site for residue CLR A 1206
ChainResidue
ATYR70
ASER74
ACYS77
AILE154
ATRP158

site_idAC7
Number of Residues2
Detailsbinding site for residue OLC A 1207
ChainResidue
ATRP122
AVAL160

site_idAC8
Number of Residues4
Detailsbinding site for residue OLC A 1208
ChainResidue
AASP130
APHE133
ALEU144
ALEU145

site_idAC9
Number of Residues3
Detailsbinding site for residue OLC A 1209
ChainResidue
AILE55
AGLN65
ATHR73

site_idAD1
Number of Residues6
Detailsbinding site for residue OLC A 1210
ChainResidue
APHE49
AVAL52
AGLN197
AVAL297
ALEU339
AOLA1214

site_idAD2
Number of Residues2
Detailsbinding site for residue OLC A 1211
ChainResidue
AALA59
AOLA1214

site_idAD3
Number of Residues3
Detailsbinding site for residue OLC A 1212
ChainResidue
ATRP173
AASN196
ALEU340

site_idAD4
Number of Residues2
Detailsbinding site for residue OLC A 1213
ChainResidue
APHE223
ALYS273

site_idAD5
Number of Residues3
Detailsbinding site for residue OLA A 1214
ChainResidue
ATHR56
AOLC1210
AOLC1211

site_idAD6
Number of Residues4
Detailsbinding site for residue OLA A 1215
ChainResidue
AMET96
ATHR100
APHE101
APHE217

site_idAD7
Number of Residues1
Detailsbinding site for residue OLA A 1216
ChainResidue
ATRP313

site_idAD8
Number of Residues1
Detailsbinding site for residue OLA A 1217
ChainResidue
ATHR283

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 Residues70
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AMET1-VAL34
AMET96-CYS106
AARG175-ASN196
AGLN299-LYS305

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AGLY35-ILE58

site_idSWS_FT_FI3
Number of Residues32
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AALA59-PHE71
AASP130-ALA150

site_idSWS_FT_FI4
Number of Residues23
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AILE72-LEU95

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLU107-VAL129

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AARG151-TYR174

site_idSWS_FT_FI7
Number of Residues23
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLN197-SER220

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU275-ILE298

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AGLU306-SER329

site_idSWS_FT_FI10
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
ChainResidueDetails
AASP113
ATHR118
AASN293
AASN312
ATYR316

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1
ChainResidueDetails
ASER203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:8521811
ChainResidueDetails
ATYR141

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:11146000
ChainResidueDetails
ASER345
ASER346

site_idSWS_FT_FI14
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS265

site_idSWS_FT_FI15
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942
ChainResidueDetails
ACYS341

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN6
AASN15

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon