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3RZE

Structure of the human histamine H1 receptor in complex with doxepin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 5EH A 1200
ChainResidue
AASP107
ATYR108
ASER111
ATHR112
ATRP158
ATRP428
ATYR431
APHE432
ATYR458

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE D7V A 1201
ChainResidue
AASP107
ATYR108
ASER111
ATHR112
AILE115
ATRP158
AASN198
ATRP428
ATYR431
APHE432
APHE435
ATYR458

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 1202
ChainResidue
AASP178
ALYS179
ALYS191
ATYR431
APHE435
AHIS450

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1203
ChainResidue
AARG1076
AARG1080

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PO4 A 1204
ChainResidue
ATHR1142
APRO1143
AASN1144
AARG1145

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 1205
ChainResidue
AGLU1011
AARG1014
AASN1053
AASN1055

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfSVFILCIDRYRsV
ChainResidueDetails
AALA113-VAL129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
ALEU30-VAL52

site_idSWS_FT_FI2
Number of Residues44
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21697825
ChainResidueDetails
AARG53-GLY62
AASP124-ARG143
ACYS471-SER487

site_idSWS_FT_FI3
Number of Residues20
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
AASN63-MET83

site_idSWS_FT_FI4
Number of Residues52
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:21697825
ChainResidueDetails
AASN84-LEU101
ATRP165-TRP189
AALA439-HIS450

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
APHE102-ILE123

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AALA144-GLY164

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
APHE190-TYR210

site_idSWS_FT_FI8
Number of Residues21
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ALEU417-ILE438

site_idSWS_FT_FI9
Number of Residues19
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AMET451-LEU470

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:15328002
ChainResidueDetails
ATHR140
ATHR142

site_idSWS_FT_FI11
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI13
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

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PDB entries from 2024-04-24

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