Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1YMG

The Channel Architecture of Aquaporin O at 2.2 Angstrom Resolution

Replaces:  1TM8
Functional Information from GO Data
ChainGOidnamespacecontents
A0002088biological_processlens development in camera-type eye
A0005212molecular_functionstructural constituent of eye lens
A0005516molecular_functioncalmodulin binding
A0005783cellular_componentendoplasmic reticulum
A0005886cellular_componentplasma membrane
A0005921cellular_componentgap junction
A0006833biological_processwater transport
A0007601biological_processvisual perception
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0045785biological_processpositive regulation of cell adhesion
A0051289biological_processprotein homotetramerization
A0055085biological_processtransmembrane transport
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 Residues66
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AMET1-SER8
ASER79-LEU84
ATHR148-SER159
AASP220-LEU263

site_idSWS_FT_FI2
Number of Residues121
DetailsTRANSMEM: Helical
ChainResidueDetails
APHE9-LEU32
ALEU39-HIS61
AARG85-VAL107
AVAL127-ALA147
AVAL160-MET176
AHIS201-TYR219

site_idSWS_FT_FI3
Number of Residues28
DetailsTOPO_DOM: Extracellular
ChainResidueDetails
AARG33-PRO38
ATHR108-SER126
ATHR195-ASN200

site_idSWS_FT_FI4
Number of Residues11
DetailsINTRAMEM:
ChainResidueDetails
AILE62-VAL67
ATYR177-MET183

site_idSWS_FT_FI5
Number of Residues20
DetailsINTRAMEM: Helical
ChainResidueDetails
AASN68-GLY78
AASN184-LEU194

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for water channel gating
ChainResidueDetails
ATYR149

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Interaction with BFSP1 => ECO:0000269|PubMed:28259670
ChainResidueDetails
AASN246

site_idSWS_FT_FI8
Number of Residues1
DetailsSITE: interaction with BFSP1 => ECO:0000269|PubMed:28259670
ChainResidueDetails
AGLU250

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:9375569
ChainResidueDetails
ASER235

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:2176601
ChainResidueDetails
ASER243

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:2176601
ChainResidueDetails
ASER245

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Deamidated asparagine => ECO:0000269|PubMed:2176601
ChainResidueDetails
AASN246

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon