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6MGW

Structure of mechanically activated ion channel OSCA1.2 in LMNG

Functional Information from GO Data
ChainGOidnamespacecontents
A0005227molecular_functioncalcium-activated cation channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0008381molecular_functionmechanosensitive monoatomic ion channel activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0098655biological_processmonoatomic cation transmembrane transport
B0005227molecular_functioncalcium-activated cation channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0008381molecular_functionmechanosensitive monoatomic ion channel activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0098655biological_processmonoatomic cation transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS01319
Number of Residues22
DetailsRBFA Ribosome-binding factor A signature. VQSlAtiegi.VKaAPFLkFivD
ChainResidueDetails
AVAL396-ASP417

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues224
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:30382939
ChainResidueDetails
AMET1-ASP6
BGLN489-ALA526
BMET589-LEU591
BTHR648-HIS650
APRO122-ARG158
AGLN397-GLY427
AGLN489-ALA526
AMET589-LEU591
ATHR648-HIS650
BMET1-ASP6
BPRO122-ARG158
BGLN397-GLY427

site_idSWS_FT_FI2
Number of Residues440
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AILE7-VAL27
AVAL627-GLY647
AALA651-PHE671
BILE7-VAL27
BILE101-VAL121
BPHE159-LYS179
BLEU376-VAL396
BPHE428-MET448
BTYR468-GLU488
BGLY527-PHE547
BTHR568-PRO588
AILE101-VAL121
BPRO592-VAL612
BVAL627-GLY647
BALA651-PHE671
APHE159-LYS179
ALEU376-VAL396
APHE428-MET448
ATYR468-GLU488
AGLY527-PHE547
ATHR568-PRO588
APRO592-VAL612

site_idSWS_FT_FI3
Number of Residues832
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:30382939
ChainResidueDetails
ALEU28-ARG100
BLEU548-ASN567
BTYR613-ASP626
BCYS672-VAL771
AGLU180-ARG375
ASER449-ARG467
ALEU548-ASN567
ATYR613-ASP626
ACYS672-VAL771
BLEU28-ARG100
BGLU180-ARG375
BSER449-ARG467

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PDB entries from 2024-04-24

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