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2BJ0

Crystal Structure of AChBP from Bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005216molecular_functionmonoatomic ion channel activity
A0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
B0004888molecular_functiontransmembrane signaling receptor activity
B0005216molecular_functionmonoatomic ion channel activity
B0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
C0004888molecular_functiontransmembrane signaling receptor activity
C0005216molecular_functionmonoatomic ion channel activity
C0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
D0004888molecular_functiontransmembrane signaling receptor activity
D0005216molecular_functionmonoatomic ion channel activity
D0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
E0004888molecular_functiontransmembrane signaling receptor activity
E0005216molecular_functionmonoatomic ion channel activity
E0005230molecular_functionextracellular ligand-gated monoatomic ion channel activity
E0006811biological_processmonoatomic ion transport
E0016020cellular_componentmembrane
E0034220biological_processmonoatomic ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CXS A1204
ChainResidue
ATRP142
BVAL103
BVAL113
ATYR184
ASER185
ACYS186
ACYS187
ATYR191
AHOH2034
BTRP51
BGLN53

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CXS B1204
ChainResidue
BTRP142
BTYR184
BSER185
BCYS186
BCYS187
BTYR191
BHOH2039
CTRP51
CGLN53
CVAL103
CVAL113

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CXS C1204
ChainResidue
CTYR88
CTRP142
CTYR184
CSER185
CCYS186
CTYR191
DTRP51
DGLN53
DVAL103
DVAL113
DHOH2048

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CXS D1204
ChainResidue
DTRP142
DTYR184
DSER185
DCYS186
DCYS187
DTYR191
DHOH2036
ETRP51
EGLN53
EVAL103
EVAL113

246031

PDB entries from 2025-12-10

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