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8YN2

Cryo-EM structure of histamine H1 receptor in complex with histamine and miniGq

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfSVFILCIDRYRsV
ChainResidueDetails
RALA113-VAL129

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299
BVAL327-GLY341

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:21697825
ChainResidueDetails
RMET1-PRO29
RMET90-ARG97
RTRP165-THR188
RCYS441-ASN446

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RLEU30-TYR50

site_idSWS_FT_FI3
Number of Residues254
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21697825
ChainResidueDetails
RALA51-LEU64
RASP124-ALA144
RLYS212-GLN416
RLEU470-SER487

site_idSWS_FT_FI4
Number of Residues24
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTYR65-LEU89

site_idSWS_FT_FI5
Number of Residues25
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RPRO98-ILE123

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=4 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RSER145-GLY164

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTRP189-ALA211

site_idSWS_FT_FI8
Number of Residues23
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RLEU417-PHE440

site_idSWS_FT_FI9
Number of Residues22
DetailsTRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RGLU447-PRO469

site_idSWS_FT_FI10
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:33828102
ChainResidueDetails
RASP107
RASN198

site_idSWS_FT_FI11
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:33828102, ECO:0007744|PDB:7DFL
ChainResidueDetails
RTHR112
RTYR431

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:15328002
ChainResidueDetails
RTHR140
RTHR142

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
RSER230

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
RTHR279

site_idSWS_FT_FI15
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P70174
ChainResidueDetails
RSER344
RSER347
RSER380

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15328002
ChainResidueDetails
RSER396
RSER398

site_idSWS_FT_FI17
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN5
RASN18

227344

PDB entries from 2024-11-13

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