4EZ1

Crystal structure of acetylcholine binding protein (AChBP) from Aplysia Californica in complex with alpha-conotoxin BuIA

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	2
Details	BINDING SITE FOR RESIDUE NH2 K 14

Chain	Residue
B	GLN57
K	CYS13

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NH2 L 14

Chain	Residue
A	ARG59
L	CYS13

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NH2 M 14

Chain	Residue
E	ASP159
M	CYS13

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NH2 N 14

Chain	Residue
D	MET116
N	ALA9
N	CYS13

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NH2 O 14

Chain	Residue
C	GLN57
C	ARG59
O	CYS13

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MN C 301

Chain	Residue
C	ASP-3
C	HIS1

---

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR CHAIN K OF ALPHA-CONOTOXIN BUIA

Chain	Residue
B	GLN57
B	MET116
B	ILE118
B	ASP164
B	SER167
C	TYR93
C	SER146
C	TRP147
C	VAL148
C	TYR149
C	TYR188
C	CYS191
C	PRO192
C	GLU193
C	TYR195
C	HOH438
K	NH214

---

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR CHAIN L OF ALPHA-CONOTOXIN BUIA

Chain	Residue
A	THR36
A	GLN57
A	ARG59
A	VAL108
A	MET116
A	ILE118
A	ASP164
A	SER166
A	SER167
B	TYR93
B	SER146
B	TRP147
B	TYR149
B	TYR188
B	CYS190
B	CYS191
B	GLU193
B	TYR195
B	HOH329
L	NH214

---

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR CHAIN M OF ALPHA-CONOTOXIN BUIA

Chain	Residue
A	TYR93
A	SER146
A	TRP147
A	VAL148
A	TYR149
A	TYR188
A	CYS190
A	CYS191
A	PRO192
A	GLU193
A	TYR195
E	TYR55
E	GLN57
E	ARG79
E	VAL108
E	MET116
E	ILE118
E	ASP164
E	SER166
E	SER167
M	NH214

---

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR CHAIN N OF ALPHA-CONOTOXIN BUIA

Chain	Residue
D	GLN57
D	ARG59
D	VAL108
D	MET116
D	ILE118
D	ASP164
D	SER166
D	SER167
E	TYR93
E	SER146
E	TRP147
E	VAL148
E	TYR149
E	TYR188
E	CYS190
E	CYS191
E	PRO192
E	GLU193
E	TYR195
E	HOH301
N	NH214

---

site_id	BC2
Number of Residues	17
Details	BINDING SITE FOR CHAIN O OF ALPHA-CONOTOXIN BUIA

Chain	Residue
D	TYR93
D	SER146
D	TRP147
D	VAL148
D	TYR149
D	TYR188
D	CYS191
D	GLU193
D	TYR195
D	HOH306
O	NH214
A	SER189
C	GLN57
C	VAL108
C	MET116
C	ASP164
C	SER167

---

Functional Information from PROSITE/UniProt

site_id	PS60014
Number of Residues	12
Details	ALPHA_CONOTOXIN Alpha-conotoxin family signature. CCStPPCAv...LYC

Chain	Residue	Details
K	CYS2-CYS13

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI6
Number of Residues	60
Details	Peptide: {"description":"Alpha-conotoxin BuIA","featureId":"PRO_0000034870","evidences":[{"source":"PubMed","id":"15520009","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964981","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16979596","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17445276","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20739611","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	5
Details	Site: {"description":"Critical residue for distinguishing between alpha-6-beta-2/CHRNA6-CHRNB2 and alpha-6-beta-4/CHRNA6-CHRNB4 nAChR subunits","evidences":[{"source":"PubMed","id":"20739611","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	5
Details	Modified residue: {"description":"Cysteine amide","evidences":[{"source":"PubMed","id":"15520009","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16964981","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16979596","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17445276","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"20739611","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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