Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3WIP

Crystal structure of acetylcholine bound to Ls-AChBP

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
F	0004888	molecular_function	transmembrane signaling receptor activity
F	0005216	molecular_function	monoatomic ion channel activity
F	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
F	0006811	biological_process	monoatomic ion transport
F	0016020	cellular_component	membrane
F	0034220	biological_process	monoatomic ion transmembrane transport
G	0004888	molecular_function	transmembrane signaling receptor activity
G	0005216	molecular_function	monoatomic ion channel activity
G	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
G	0006811	biological_process	monoatomic ion transport
G	0016020	cellular_component	membrane
G	0034220	biological_process	monoatomic ion transmembrane transport
H	0004888	molecular_function	transmembrane signaling receptor activity
H	0005216	molecular_function	monoatomic ion channel activity
H	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
H	0006811	biological_process	monoatomic ion transport
H	0016020	cellular_component	membrane
H	0034220	biological_process	monoatomic ion transmembrane transport
I	0004888	molecular_function	transmembrane signaling receptor activity
I	0005216	molecular_function	monoatomic ion channel activity
I	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
I	0006811	biological_process	monoatomic ion transport
I	0016020	cellular_component	membrane
I	0034220	biological_process	monoatomic ion transmembrane transport
J	0004888	molecular_function	transmembrane signaling receptor activity
J	0005216	molecular_function	monoatomic ion channel activity
J	0005230	molecular_function	extracellular ligand-gated monoatomic ion channel activity
J	0006811	biological_process	monoatomic ion transport
J	0016020	cellular_component	membrane
J	0034220	biological_process	monoatomic ion transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACH A 301

Chain	Residue
A	TYR89
A	TRP143
A	TYR185
A	TYR192
B	MET114

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 1PE A 302

Chain	Residue
A	TRP65
H	ASN9
H	LEU63
H	ALA64
H	TRP65
A	ASN9
A	THR13
A	LEU63
A	ALA64

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE 1PE A 303

Chain	Residue
A	ILE36
A	ASN37
A	VAL51
A	TRP53
A	SER116
A	TYR164
A	SER166
A	HOH417
E	TYR89
E	ASN90
E	ALA91
E	ILE92
E	SER122
E	TRP143
E	TYR185

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE A 304

Chain	Residue
A	GLN54
A	LEU86
A	ALA88
A	TYR89
A	ALA91
A	TYR113
A	ILE117
A	GLN119
B	LEU98
B	SER116

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACH B 301

Chain	Residue
B	TYR89
B	TRP143
B	TYR192
C	TRP53
C	MET114

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 302

Chain	Residue
A	THR21
A	ASP24
B	ASP2
B	ARG3

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1PE B 303

Chain	Residue
B	TYR89
B	ALA91
B	TRP143
B	HOH415
C	ILE36
C	TRP53
C	SER116
C	TYR164

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 1PE B 304

Chain	Residue
B	ILE6
B	ASN9
B	THR13
B	THR62
B	LEU63
B	ALA64
B	TRP65
G	LEU1
G	ASN9
G	THR13
G	THR62
G	LEU63
G	TRP65

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT B 305

Chain	Residue
B	PRO71
B	ASP72

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACH C 301

Chain	Residue
C	TYR89
C	TRP143
C	TYR185
C	TYR192
D	TRP53

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 302

Chain	Residue
C	ARG15
D	ALA4
D	ASP5
F	ALA4
F	ASP5
J	ARG15

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACH D 301

Chain	Residue
D	TYR89
D	TRP143
D	TYR185
E	TRP53
E	MET114

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 302

Chain	Residue
C	THR21
C	ASP24
D	ASP2
D	ARG3
D	PRO71

site_id	BC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE D 303

Chain	Residue
E	VAL74
E	SER75
E	GLN101
D	ASP17
D	ILE19
D	TRP82
D	VAL83
D	HIS145
D	HOH441
E	ARG3

site_id	BC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1PE D 304

Chain	Residue
C	ALA88
C	TYR89
C	ALA91
C	TRP143
C	TYR185
D	ILE36
D	TRP53
D	LEU98
D	SER116
D	GLU163
D	TYR164
D	HOH434

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACH E 301

Chain	Residue
E	TYR89
E	TRP143
E	TYR185
E	TYR192

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 302

Chain	Residue
D	ARG148
E	ARG3
E	PRO71
E	ASP72

site_id	BC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 1PE E 303

Chain	Residue
A	ARG3
A	LEU7
A	GLN73
A	VAL74
A	SER75
A	LEU102
E	PRO16
E	ASP17
E	ILE19
E	ILE78
E	LEU81
E	TRP82
E	VAL83
E	HIS145

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACH F 301

Chain	Residue
F	TYR89
F	TRP143
F	TYR185
F	TYR192

site_id	CC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 F 302

Chain	Residue
F	ASP2
F	ARG3
F	PRO71
J	THR21
J	ASP24
J	HOH428

site_id	CC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACH G 301

Chain	Residue
G	TYR89
G	TRP143
G	TYR185
H	LEU112

site_id	CC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 G 302

Chain	Residue
F	THR21
G	ASP2
G	ARG3

site_id	CC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE G 303

Chain	Residue
B	ARG15
C	ASP5
C	TYR8
C	ASN9
F	THR13
F	ARG15
G	LEU1
G	ALA4
G	ASP5
G	TYR8
G	ASN9

site_id	CC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL G 304

Chain	Residue
G	ASN66

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT G 305

Chain	Residue
G	ASP129
G	ARG170
G	LYS203

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT G 306

Chain	Residue
G	ARG148
H	ASP72
H	GLN73

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACH H 301

Chain	Residue
H	TYR89
H	TRP143
H	TYR185
H	TYR192

site_id	DC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 1PE H 302

Chain	Residue
H	ASP17
H	ILE19
H	TRP82
H	VAL83
H	ASP85
H	HIS145
I	ARG3
I	LEU7
I	GLN73
I	VAL74
I	SER75
I	LEU102

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACH I 301

Chain	Residue
I	TYR89
I	TRP143
I	TYR185
J	TRP53

site_id	DC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE I 302

Chain	Residue
E	ASN9
E	LEU63
E	ALA64
I	LEU1
I	ASN9
I	ILE10
I	THR62
I	LEU63
I	ALA64
I	TRP65

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACH J 301

Chain	Residue
F	MET114
J	TYR89
J	TRP143
J	TYR185
J	TYR192

site_id	DC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 J 302

Chain	Residue
J	ASP129
J	ARG170
J	LYS203

site_id	DC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 1PE J 303

Chain	Residue
D	ASN9
D	THR13
D	THR62
D	ALA64
D	TRP65
J	ASN9
J	ILE10
J	THR13
J	LEU63
J	ALA64
J	TRP65

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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