Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6SSI

Structure of the pentameric ligand-gated ion channel ELIC in complex with a PAM nanobody

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004888	molecular_function	transmembrane signaling receptor activity
A	0005216	molecular_function	monoatomic ion channel activity
A	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
A	0006811	biological_process	monoatomic ion transport
A	0016020	cellular_component	membrane
A	0034220	biological_process	monoatomic ion transmembrane transport
B	0004888	molecular_function	transmembrane signaling receptor activity
B	0005216	molecular_function	monoatomic ion channel activity
B	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
B	0006811	biological_process	monoatomic ion transport
B	0016020	cellular_component	membrane
B	0034220	biological_process	monoatomic ion transmembrane transport
C	0004888	molecular_function	transmembrane signaling receptor activity
C	0005216	molecular_function	monoatomic ion channel activity
C	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
C	0006811	biological_process	monoatomic ion transport
C	0016020	cellular_component	membrane
C	0034220	biological_process	monoatomic ion transmembrane transport
D	0004888	molecular_function	transmembrane signaling receptor activity
D	0005216	molecular_function	monoatomic ion channel activity
D	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
D	0006811	biological_process	monoatomic ion transport
D	0016020	cellular_component	membrane
D	0034220	biological_process	monoatomic ion transmembrane transport
E	0004888	molecular_function	transmembrane signaling receptor activity
E	0005216	molecular_function	monoatomic ion channel activity
E	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
E	0006811	biological_process	monoatomic ion transport
E	0016020	cellular_component	membrane
E	0034220	biological_process	monoatomic ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue ABU A 401

Chain	Residue
A	GLU131
A	PRO132
A	PHE133
A	TYR175
A	PHE188
B	ARG91
B	GOL403

site_id	AC2
Number of Residues	2
Details	binding site for residue MES A 402

Chain	Residue
A	GLY45
A	TRP72

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 403

Chain	Residue
A	PHE19
A	TYR38
A	VAL40
A	ASN103
E	TYR175
E	HIS177
E	ABU401

site_id	AC4
Number of Residues	3
Details	binding site for residue CA A 404

Chain	Residue
A	ASP153
A	GLU155
A	ASP158

site_id	AC5
Number of Residues	9
Details	binding site for residue ABU B 401

Chain	Residue
B	GLU131
B	PRO132
B	PHE133
B	TYR175
B	HIS177
B	PHE188
C	ARG91
C	ASN103
C	GOL403

site_id	AC6
Number of Residues	3
Details	binding site for residue MES B 402

Chain	Residue
B	GLY45
B	TRP72
B	HOH512

site_id	AC7
Number of Residues	6
Details	binding site for residue GOL B 403

Chain	Residue
A	PHE133
A	HIS177
A	ABU401
B	TYR38
B	ARG91
B	ASN103

site_id	AC8
Number of Residues	9
Details	binding site for residue PG4 B 404

Chain	Residue
B	ILE39
B	ILE63
B	PRO74
B	ALA75
B	LEU76
B	THR87
B	LYS90
B	TYR102
B	HOH506

site_id	AC9
Number of Residues	3
Details	binding site for residue CA B 405

Chain	Residue
B	ASP153
B	GLU155
B	ASP158

site_id	AD1
Number of Residues	4
Details	binding site for residue UMQ B 406

Chain	Residue
A	THR259
A	GLN264
B	GLU156
B	TRP206

site_id	AD2
Number of Residues	5
Details	binding site for residue UMQ B 407

Chain	Residue
B	THR259
B	GLN264
B	PHE308
C	GLU156
C	TRP206

site_id	AD3
Number of Residues	8
Details	binding site for residue ABU C 401

Chain	Residue
C	GLU131
C	PRO132
C	PHE133
C	TYR175
C	PHE188
C	HOH512
D	ARG91
D	GOL403

site_id	AD4
Number of Residues	3
Details	binding site for residue MES C 402

Chain	Residue
C	GLY45
C	TRP72
C	HOH516

site_id	AD5
Number of Residues	4
Details	binding site for residue GOL C 403

Chain	Residue
B	ABU401
C	TYR38
C	VAL40
C	ASN103

site_id	AD6
Number of Residues	6
Details	binding site for residue PG4 C 404

Chain	Residue
C	SER111
C	ASN112
C	GLU129
C	ILE173
C	ARG174
C	ARG190

site_id	AD7
Number of Residues	3
Details	binding site for residue CA C 405

Chain	Residue
C	ASP153
C	GLU155
C	ASP158

site_id	AD8
Number of Residues	4
Details	binding site for residue UMQ C 406

Chain	Residue
C	THR259
C	GLN264
C	ILE267
D	SER202

site_id	AD9
Number of Residues	8
Details	binding site for residue ABU D 401

Chain	Residue
D	GLU131
D	PRO132
D	PHE133
D	TYR175
D	HIS177
D	PHE188
E	ARG91
E	GOL403

site_id	AE1
Number of Residues	5
Details	binding site for residue MES D 402

Chain	Residue
D	GLY45
D	LYS46
D	TRP72
D	TYR135
D	HOH505

site_id	AE2
Number of Residues	4
Details	binding site for residue GOL D 403

Chain	Residue
C	HIS177
C	ABU401
D	TYR38
D	ASN103

site_id	AE3
Number of Residues	5
Details	binding site for residue PG4 D 404

Chain	Residue
D	ILE39
D	PRO74
D	LEU76
D	LYS90
D	TYR102

site_id	AE4
Number of Residues	3
Details	binding site for residue CA D 405

Chain	Residue
D	ASP153
D	GLU155
D	ASP158

site_id	AE5
Number of Residues	3
Details	binding site for residue ACT D 406

Chain	Residue
C	SER84
D	ASP86
D	THR87

site_id	AE6
Number of Residues	8
Details	binding site for residue ABU E 401

Chain	Residue
A	ARG91
A	GOL403
E	GLU131
E	PRO132
E	PHE133
E	TYR175
E	HIS177
E	GOL404

site_id	AE7
Number of Residues	3
Details	binding site for residue MES E 402

Chain	Residue
E	GLY45
E	LYS46
E	TRP72

site_id	AE8
Number of Residues	6
Details	binding site for residue GOL E 403

Chain	Residue
D	HIS177
D	ABU401
E	PHE19
E	TYR38
E	VAL40
E	ASN103

site_id	AE9
Number of Residues	7
Details	binding site for residue GOL E 404

Chain	Residue
A	ARG91
A	MET93
E	SER134
E	ASN136
E	LEU178
E	GLN185
E	ABU401

site_id	AF1
Number of Residues	7
Details	binding site for residue PG4 E 405

Chain	Residue
E	ILE63
E	VAL73
E	PRO74
E	ALA75
E	LEU76
E	LYS90
E	TYR102

site_id	AF2
Number of Residues	4
Details	binding site for residue CA E 406

Chain	Residue
D	ASP113
E	ASP153
E	GLU155
E	ASP158

site_id	AF3
Number of Residues	3
Details	binding site for residue ACT E 407

Chain	Residue
D	SER84
E	ASP86
E	THR87

site_id	AF4
Number of Residues	5
Details	binding site for residue UMQ E 408

Chain	Residue
A	SER202
A	TRP206
E	THR259
E	GLN264
E	ILE267

site_id	AF5
Number of Residues	7
Details	binding site for residue UMQ E 409

Chain	Residue
D	THR259
D	GLN264
D	ILE267
D	ILE311
E	GLU156
E	SER202
E	TRP206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	300
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	35
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	45
Details	Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	40
Details	Motif: {"description":"Cys-loop"}

Chain

Residue

Details

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