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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
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues27
DetailsIntramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2B6O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues10
DetailsRegion: {"description":"Interaction with CALM","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsMotif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsMotif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Important for water channel gating","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Cleavage; promotes interactions between tetramers from adjoining membranes","evidences":[{"source":"PubMed","id":"15351655","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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