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6HY7

Crystal structure of alpha9 nAChR extracellular domain in complex with alpha-conotoxin RgIA

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
A0022848molecular_functionacetylcholine-gated monoatomic cation-selective channel activity
A0034220biological_processmonoatomic ion transmembrane transport
A0045211cellular_componentpostsynaptic membrane
Functional Information from PROSITE/UniProt
site_idPS00236
Number of Residues15
DetailsNEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CvVdVtyFPfDnqqC
ChainResidueDetails
ACYS130-CYS144

site_idPS60014
Number of Residues11
DetailsALPHA_CONOTOXIN Alpha-conotoxin family signature. CCSdPRCR....YRC
ChainResidueDetails
BCYS2-CYS12

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Key residue for potent inhibition of the rat CHRNA9-CHRNA10 nAChR => ECO:0000269|PubMed:18295795
ChainResidueDetails
BASP5
BPRO6
BARG7
BARG9

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Binds to the Glu-221 of the rat nAChR CHRNA10 subunit => ECO:0000305|PubMed:25740413
ChainResidueDetails
BARG11

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN32
AASN145

218500

数据于2024-04-17公开中

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