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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 Residues121
DetailsTRANSMEM: Helical
ChainResidueDetails
APHE9-LEU32
ALEU39-HIS61
AARG85-VAL107
AVAL127-ALA147
AVAL160-MET176
AHIS201-TYR219

site_idSWS_FT_FI2
Number of Residues28
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AARG33-PRO38
ATHR108-SER126
ATHR195-ASN200

site_idSWS_FT_FI3
Number of Residues11
DetailsINTRAMEM:
ChainResidueDetails
AILE62-VAL67
ATYR177-MET183

site_idSWS_FT_FI4
Number of Residues20
DetailsINTRAMEM: Helical
ChainResidueDetails
AASN68-GLY78
AASN184-LEU194

site_idSWS_FT_FI5
Number of Residues16
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
ASER79-LEU84
ATHR148-SER159

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for water channel gating => ECO:0000250
ChainResidueDetails
ATYR149

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06624
ChainResidueDetails
ASER235

218853

PDB entries from 2024-04-24

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