Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3RZE

Structure of the human histamine H1 receptor in complex with doxepin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003796	molecular_function	lysozyme activity
A	0004930	molecular_function	G protein-coupled receptor activity
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009253	biological_process	peptidoglycan catabolic process
A	0016020	cellular_component	membrane
A	0016998	biological_process	cell wall macromolecule catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 5EH A 1200

Chain	Residue
A	ASP107
A	TYR108
A	SER111
A	THR112
A	TRP158
A	TRP428
A	TYR431
A	PHE432
A	TYR458

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE D7V A 1201

Chain	Residue
A	ASP107
A	TYR108
A	SER111
A	THR112
A	ILE115
A	TRP158
A	ASN198
A	TRP428
A	TYR431
A	PHE432
A	PHE435
A	TYR458

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 1202

Chain	Residue
A	ASP178
A	LYS179
A	LYS191
A	TYR431
A	PHE435
A	HIS450

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 A 1203

Chain	Residue
A	ARG1076
A	ARG1080

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 A 1204

Chain	Residue
A	THR1142
A	PRO1143
A	ASN1144
A	ARG1145

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE OLC A 1205

Chain	Residue
A	GLU1011
A	ARG1014
A	ASN1053
A	ASN1055

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIfSVFILCIDRYRsV

Chain	Residue	Details
A	ALA113-VAL129

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	33
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"21697825","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	12
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"21697825","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	25
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	9
Details	Region: {"description":"Important for agonist binding","evidences":[{"source":"PubMed","id":"21697825","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	34
Details	Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	16
Details	Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33828102","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DFL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15328002","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	3
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P70174","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15328002","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 921

Chain	Residue	Details
A	GLU1011	proton shuttle (general acid/base)
A	ASP1020	covalent catalysis

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)