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2B6O

Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state

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 PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MC3 A 264
ChainResidue
AARG196
AMC3269
AMC3270
AMC3272
AHOH273
AHOH304

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MC3 A 265
ChainResidue
ASER106
AMC3270
AHOH291
AHOH301
AHOH327
AALA102
AVAL103
ATYR105

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MC3 A 266
ChainResidue
ALEU83
ALEU84
AILE87
AVAL90
AVAL91
ALEU94
ALYS238
AMC3267
AMC3271

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MC3 A 267
ChainResidue
AARG5
ASER6
APHE9
ATRP10
ALEU84
ACYS88
AMC3266
AMC3272

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MC3 A 268
ChainResidue
AALA7
ATRP10
AARG11
APHE14

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MC3 A 269
ChainResidue
AMC3264
AMC3272

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MC3 A 270
ChainResidue
ALEU95
ATYR105
AILE193
ALEU194
AARG196
AMC3264
AMC3265
AHOH326

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MC3 A 271
ChainResidue
AMC3266

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MC3 A 272
ChainResidue
AMC3264
AMC3267
AMC3269

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

238582

PDB entries from 2025-07-09

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