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8SJX

Structure of lens aquaporin-0 array in sphingomyelin/cholesterol bilayer (2SM:1Chol)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002088biological_processlens development in camera-type eye
A0005212molecular_functionstructural constituent of eye lens
A0005516molecular_functioncalmodulin binding
A0005886cellular_componentplasma membrane
A0006833biological_processwater transport
A0007601biological_processvisual perception
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0034109biological_processhomotypic cell-cell adhesion
A0036438biological_processmaintenance of lens transparency
A0055085biological_processtransmembrane transport
A0070161cellular_componentanchoring junction
A0098631molecular_functioncell adhesion mediator activity
A1990349biological_processgap junction-mediated intercellular transport
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGAGLGSLLYdFllfprlksvserl.....SILK
ChainResidueDetails
AILE210-LYS238

site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HVNPAVTFA
ChainResidueDetails
AHIS66-ALA74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16319884
ChainResidueDetails
AMET1-ALA12
AGLY60-SER63
AVAL77-ARG85
ATHR148-LEU157
ATYR219-LEU263

site_idSWS_FT_FI2
Number of Residues17
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AILE13-ALA30

site_idSWS_FT_FI3
Number of Residues35
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:16319884
ChainResidueDetails
ASER31-HIS40
AVAL107-SER126
AMET176-TYR177
ALEU194-ASN200

site_idSWS_FT_FI4
Number of Residues18
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AVAL41-VAL59

site_idSWS_FT_FI5
Number of Residues27
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AGLY64-LEU76
ATYR178-ILE193

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AALA86-SER106

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AVAL127-ALA147

site_idSWS_FT_FI8
Number of Residues17
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AGLY158-GLY175

site_idSWS_FT_FI9
Number of Residues17
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AHIS201-LEU218

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Important for water channel gating => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
ATYR149

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Cleavage; promotes interactions between tetramers from adjoining membranes => ECO:0000269|PubMed:15351655
ChainResidueDetails
ALEU234
ASER243

site_idSWS_FT_FI12
Number of Residues1
DetailsSITE: Interaction with BFSP1 => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
AASN246

site_idSWS_FT_FI13
Number of Residues1
DetailsSITE: interaction with BFSP1 => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
AGLU250

site_idSWS_FT_FI14
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
ASER235
ASER243
ASER245

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PDB entries from 2025-07-02

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