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1SOR

Aquaporin-0 membrane junctions reveal the structure of a closed water pore

Functional Information from GO Data
ChainGOidnamespacecontents
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane 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 Residues17
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AILE13-ALA30

site_idSWS_FT_FI2
Number of Residues35
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:16319884
ChainResidueDetails
ASER31-HIS40
AVAL107-SER126
AMET176-TYR177
ALEU194-ASN200

site_idSWS_FT_FI3
Number of Residues18
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:16319884, ECO:0007744|PDB:2B6O
ChainResidueDetails
AVAL41-VAL59

site_idSWS_FT_FI4
Number of Residues20
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16319884
ChainResidueDetails
AGLY60-SER63
AVAL77-ARG85
ATHR148-LEU157

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 Residues1
DetailsSITE: Cleavage; promotes interactions between tetramers from adjoining membranes => ECO:0000269|PubMed:15351655
ChainResidueDetails
ALEU234

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
ASER235

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PDB entries from 2025-06-11

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