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3C02

X-ray structure of the aquaglyceroporin from Plasmodium falciparum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006833biological_processwater transport
A0008519molecular_functionammonium channel activity
A0009247biological_processglycolipid biosynthetic process
A0015166molecular_functionpolyol transmembrane transporter activity
A0015168molecular_functionglycerol transmembrane transporter activity
A0015204molecular_functionurea transmembrane transporter activity
A0015250molecular_functionwater channel activity
A0015254molecular_functionglycerol channel activity
A0015267molecular_functionchannel activity
A0015791biological_processpolyol transmembrane transport
A0015793biological_processglycerol transmembrane transport
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0051475biological_processglucosylglycerol transmembrane transport
A0055085biological_processtransmembrane transport
A0071918biological_processurea transmembrane transport
A0072488biological_processammonium transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-ARG11
AALA67-LYS87
AASP157-SER171
AASP239-LEU258

site_idSWS_FT_FI2
Number of Residues120
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLU12-ALA32
ALEU46-GLY66
AILE88-GLY108
AGLY136-VAL156
AVAL172-LEU192
APHE218-TYR238

site_idSWS_FT_FI3
Number of Residues62
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AASN33-LYS45
ALEU109-THR135
AASN193-ASN217

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18500352, ECO:0007744|PDB:3C02
ChainResidueDetails
AGLY66
AALA67
AASN70
ASER127
AGLY189
APHE190
AASN193
AARG196

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PDB entries from 2025-06-18

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