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6NBH

Cryo-EM structure of parathyroid hormone receptor type 1 in complex with a long-acting parathyroid hormone analog and G protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003924molecular_functionGTPase activity
A0005525molecular_functionGTP binding
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0019001molecular_functionguanyl nucleotide binding
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0001750cellular_componentphotoreceptor outer segment
B0001917cellular_componentphotoreceptor inner segment
B0003924molecular_functionGTPase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0007204biological_processpositive regulation of cytosolic calcium ion concentration
B0008283biological_processcell population proliferation
B0010659biological_processcardiac muscle cell apoptotic process
B0030159molecular_functionsignaling receptor complex adaptor activity
B0030425cellular_componentdendrite
B0030507molecular_functionspectrin binding
B0042622cellular_componentphotoreceptor outer segment membrane
B0044297cellular_componentcell body
B0044877molecular_functionprotein-containing complex binding
B0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071456biological_processcellular response to hypoxia
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
P0005179molecular_functionhormone activity
P0005576cellular_componentextracellular region
P0030282biological_processbone mineralization
R0004888molecular_functiontransmembrane signaling receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0004991molecular_functionparathyroid hormone receptor activity
R0007166biological_processcell surface receptor signaling pathway
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CLR R 601
ChainResidue
RTRP322
RVAL326
RCLR607

site_idAC2
Number of Residues3
Detailsbinding site for residue CLR R 602
ChainResidue
RILE422
RALA426
RPRO428

site_idAC3
Number of Residues2
Detailsbinding site for residue CLR R 603
ChainResidue
RTRP361
RPRO428

site_idAC4
Number of Residues1
Detailsbinding site for residue CLR R 604
ChainResidue
RVAL382

site_idAC5
Number of Residues2
Detailsbinding site for residue CLR R 605
ChainResidue
RALA279
RTHR286

site_idAC6
Number of Residues2
Detailsbinding site for residue CLR R 606
ChainResidue
RASN358
RLYS359

site_idAC7
Number of Residues2
Detailsbinding site for residue CLR R 607
ChainResidue
RPHE291
RCLR601

site_idAC8
Number of Residues2
Detailsbinding site for residue PLM R 608
ChainResidue
RALA275
RTYR278

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. ClpeWDhil.CWplGapgevvavpCP
ChainResidueDetails
RCYS108-PRO132

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVaIIYCFcNgeV
ChainResidueDetails
RGLN451-VAL466

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:10427002, ECO:0000305|PubMed:11087399, ECO:0000305|PubMed:15591060, ECO:0000305|PubMed:16766715, ECO:0000305|PubMed:19243146, ECO:0000305|PubMed:9395396, ECO:0000305|PubMed:9417641
ChainResidueDetails
AGLY47
AASP223
AASN292
AALA366

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10427002, ECO:0000269|PubMed:11087399, ECO:0000269|PubMed:15591060, ECO:0000269|PubMed:19243146, ECO:0000269|PubMed:9395396, ECO:0000269|PubMed:9417641, ECO:0000305|PubMed:16766715
ChainResidueDetails
ASER54

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
RHIS307-TYR320
RARG383-SER409
ASER352

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P63092
ChainResidueDetails
ALYS300

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ALEU198
ATHR204
AASP173

site_idSWS_FT_FI6
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000250|UniProtKB:P63096
ChainResidueDetails
AGLY2

site_idSWS_FT_FI7
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS3

site_idSWS_FT_FI8
Number of Residues18
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
RTHR410-PRO428

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
RMET441-ASN463

site_idSWS_FT_FI10
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN151
RASN161
RASN166
RASN176

218500

PDB entries from 2024-04-17

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