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3M9I

Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids

Functional Information from GO Data
ChainGOidnamespacecontents
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 3PE A 301
ChainResidue
AARG196
APHE198
A3PE302

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 3PE A 302
ChainResidue
AARG196
A3PE301

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3PE A 303
ChainResidue
ALEU194
AARG196
A3PE304
A3PE306
APHE17
ALEU95
ATYR105
AILE193

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 3PE A 304
ChainResidue
ASER106
A3PE303
A3PE307

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 3PE A 306
ChainResidue
APHE9
ATRP10
AVAL91
ALEU95
A3PE303
A3PE307

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 3PE A 307
ChainResidue
AALA7
ATRP10
AILE13
APHE14
APHE17
ALEU95
A3PE304
A3PE306

Functional Information from PROSITE/UniProt
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 Residues2
DetailsMotif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsMotif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"16319884","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Important for water channel gating","evidences":[{"source":"UniProtKB","id":"P06624","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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