Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6LMT

Cryo-EM structure of the killifish CALHM1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005227	molecular_function	calcium activated cation channel activity
A	0005244	molecular_function	voltage-gated ion channel activity
A	0006812	biological_process	cation transport
B	0005227	molecular_function	calcium activated cation channel activity
B	0005244	molecular_function	voltage-gated ion channel activity
B	0006812	biological_process	cation transport
C	0005227	molecular_function	calcium activated cation channel activity
C	0005244	molecular_function	voltage-gated ion channel activity
C	0006812	biological_process	cation transport
D	0005227	molecular_function	calcium activated cation channel activity
D	0005244	molecular_function	voltage-gated ion channel activity
D	0006812	biological_process	cation transport
E	0005227	molecular_function	calcium activated cation channel activity
E	0005244	molecular_function	voltage-gated ion channel activity
E	0006812	biological_process	cation transport
F	0005227	molecular_function	calcium activated cation channel activity
F	0005244	molecular_function	voltage-gated ion channel activity
F	0006812	biological_process	cation transport
G	0005227	molecular_function	calcium activated cation channel activity
G	0005244	molecular_function	voltage-gated ion channel activity
G	0006812	biological_process	cation transport
H	0005227	molecular_function	calcium activated cation channel activity
H	0005244	molecular_function	voltage-gated ion channel activity
H	0006812	biological_process	cation transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	binding site for residue Y01 A 401

Chain	Residue
A	MET33
B	VAL116
B	MET119
B	Y01401
B	Y01404
A	SER36
A	TRP62
A	LEU66
A	VAL69
B	MET19
B	ALA111
B	VAL112
B	SER115

site_id	AC2
Number of Residues	5
Details	binding site for residue Y01 A 402

Chain	Residue
A	TYR49
A	ILE53
A	LEU56
A	PHE128
A	ASN131

site_id	AC3
Number of Residues	9
Details	binding site for residue Y01 A 403

Chain	Residue
A	MET19
A	GLN104
A	LEU107
A	ILE108
A	MET192
A	ILE199
A	ARG200
A	ARG203
A	Y01404

site_id	AC4
Number of Residues	13
Details	binding site for residue Y01 A 404

Chain	Residue
A	MET19
A	ALA111
A	VAL112
A	SER115
A	VAL116
A	MET119
A	Y01403
A	Y01405
H	MET33
H	SER36
H	TRP62
H	LEU66
H	VAL69

site_id	AC5
Number of Residues	7
Details	binding site for residue Y01 A 405

Chain	Residue
A	MET7
A	ALA27
A	LEU28
A	ALA31
A	SER35
A	Y01404
H	SER36

site_id	AC6
Number of Residues	7
Details	binding site for residue Y01 B 401

Chain	Residue
A	SER36
A	Y01401
B	MET7
B	ALA27
B	LEU28
B	ALA31
B	SER35

site_id	AC7
Number of Residues	13
Details	binding site for residue Y01 B 402

Chain	Residue
B	MET33
B	SER36
B	TRP62
B	LEU66
B	VAL69
C	MET19
C	ALA111
C	VAL112
C	SER115
C	VAL116
C	MET119
C	Y01401
C	Y01404

site_id	AC8
Number of Residues	5
Details	binding site for residue Y01 B 403

Chain	Residue
B	TYR49
B	ILE53
B	LEU56
B	PHE128
B	ASN131

site_id	AC9
Number of Residues	9
Details	binding site for residue Y01 B 404

Chain	Residue
A	Y01401
B	MET19
B	GLN104
B	LEU107
B	ILE108
B	MET192
B	ILE199
B	ARG200
B	ARG203

site_id	AD1
Number of Residues	7
Details	binding site for residue Y01 C 401

Chain	Residue
B	SER36
B	Y01402
C	MET7
C	ALA27
C	LEU28
C	ALA31
C	SER35

site_id	AD2
Number of Residues	13
Details	binding site for residue Y01 C 402

Chain	Residue
D	Y01401
D	Y01404
C	MET33
C	SER36
C	TRP62
C	LEU66
C	VAL69
D	MET19
D	ALA111
D	VAL112
D	SER115
D	VAL116
D	MET119

site_id	AD3
Number of Residues	5
Details	binding site for residue Y01 C 403

Chain	Residue
C	TYR49
C	ILE53
C	LEU56
C	PHE128
C	ASN131

site_id	AD4
Number of Residues	9
Details	binding site for residue Y01 C 404

Chain	Residue
B	Y01402
C	MET19
C	GLN104
C	LEU107
C	ILE108
C	MET192
C	ILE199
C	ARG200
C	ARG203

site_id	AD5
Number of Residues	7
Details	binding site for residue Y01 D 401

Chain	Residue
C	SER36
C	Y01402
D	MET7
D	ALA27
D	LEU28
D	ALA31
D	SER35

site_id	AD6
Number of Residues	13
Details	binding site for residue Y01 D 402

Chain	Residue
D	MET33
D	SER36
D	TRP62
D	LEU66
D	VAL69
E	MET19
E	ALA111
E	VAL112
E	SER115
E	VAL116
E	MET119
E	Y01401
E	Y01404

site_id	AD7
Number of Residues	5
Details	binding site for residue Y01 D 403

Chain	Residue
D	TYR49
D	ILE53
D	LEU56
D	PHE128
D	ASN131

site_id	AD8
Number of Residues	9
Details	binding site for residue Y01 D 404

Chain	Residue
C	Y01402
D	MET19
D	GLN104
D	LEU107
D	ILE108
D	MET192
D	ILE199
D	ARG200
D	ARG203

site_id	AD9
Number of Residues	7
Details	binding site for residue Y01 E 401

Chain	Residue
D	SER36
D	Y01402
E	MET7
E	ALA27
E	LEU28
E	ALA31
E	SER35

site_id	AE1
Number of Residues	13
Details	binding site for residue Y01 E 402

Chain	Residue
E	MET33
E	SER36
E	TRP62
E	LEU66
E	VAL69
F	MET19
F	ALA111
F	VAL112
F	SER115
F	VAL116
F	MET119
F	Y01401
F	Y01404

site_id	AE2
Number of Residues	5
Details	binding site for residue Y01 E 403

Chain	Residue
E	TYR49
E	ILE53
E	LEU56
E	PHE128
E	ASN131

site_id	AE3
Number of Residues	9
Details	binding site for residue Y01 E 404

Chain	Residue
D	Y01402
E	MET19
E	GLN104
E	LEU107
E	ILE108
E	MET192
E	ILE199
E	ARG200
E	ARG203

site_id	AE4
Number of Residues	7
Details	binding site for residue Y01 F 401

Chain	Residue
E	SER36
E	Y01402
F	MET7
F	ALA27
F	LEU28
F	ALA31
F	SER35

site_id	AE5
Number of Residues	13
Details	binding site for residue Y01 F 402

Chain	Residue
F	MET33
F	SER36
F	TRP62
F	LEU66
F	VAL69
G	MET19
G	ALA111
G	VAL112
G	SER115
G	VAL116
G	MET119
G	Y01401
G	Y01404

site_id	AE6
Number of Residues	5
Details	binding site for residue Y01 F 403

Chain	Residue
F	TYR49
F	ILE53
F	LEU56
F	PHE128
F	ASN131

site_id	AE7
Number of Residues	9
Details	binding site for residue Y01 F 404

Chain	Residue
E	Y01402
F	MET19
F	GLN104
F	LEU107
F	ILE108
F	MET192
F	ILE199
F	ARG200
F	ARG203

site_id	AE8
Number of Residues	7
Details	binding site for residue Y01 G 401

Chain	Residue
F	SER36
F	Y01402
G	MET7
G	ALA27
G	LEU28
G	ALA31
G	SER35

site_id	AE9
Number of Residues	13
Details	binding site for residue Y01 G 402

Chain	Residue
G	MET33
G	SER36
G	TRP62
G	LEU66
G	VAL69
H	MET19
H	ALA111
H	VAL112
H	SER115
H	VAL116
H	MET119
H	Y01401
H	Y01403

site_id	AF1
Number of Residues	5
Details	binding site for residue Y01 G 403

Chain	Residue
G	TYR49
G	ILE53
G	LEU56
G	PHE128
G	ASN131

site_id	AF2
Number of Residues	9
Details	binding site for residue Y01 G 404

Chain	Residue
F	Y01402
G	MET19
G	GLN104
G	LEU107
G	ILE108
G	MET192
G	ILE199
G	ARG200
G	ARG203

site_id	AF3
Number of Residues	7
Details	binding site for residue Y01 H 401

Chain	Residue
G	SER36
G	Y01402
H	MET7
H	ALA27
H	LEU28
H	ALA31
H	SER35

site_id	AF4
Number of Residues	5
Details	binding site for residue Y01 H 402

Chain	Residue
H	TYR49
H	ILE53
H	LEU56
H	PHE128
H	ASN131

site_id	AF5
Number of Residues	9
Details	binding site for residue Y01 H 403

Chain	Residue
G	Y01402
H	MET19
H	GLN104
H	LEU107
H	ILE108
H	MET192
H	ILE199
H	ARG200
H	ARG203

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	120
Details	Transmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	504
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	176
Details	Transmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	208
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	200
Details	Transmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	200
Details	Transmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LMT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	216
Details	Region: {"description":"Central pore","evidences":[{"source":"PubMed","id":"32832629","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	232
Details	Region: {"description":"Phospholipid-binding","evidences":[{"source":"UniProtKB","id":"Q8IU99","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"D3Z291","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q8IU99","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)