3C02

X-ray structure of the aquaglyceroporin from Plasmodium falciparum

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0006833	biological_process	water transport
A	0008519	molecular_function	ammonium channel activity
A	0009247	biological_process	glycolipid biosynthetic process
A	0015166	molecular_function	polyol transmembrane transporter activity
A	0015168	molecular_function	glycerol transmembrane transporter activity
A	0015204	molecular_function	urea transmembrane transporter activity
A	0015250	molecular_function	water channel activity
A	0015254	molecular_function	glycerol channel activity
A	0015267	molecular_function	channel activity
A	0015791	biological_process	polyol transmembrane transport
A	0015793	biological_process	glycerol transmembrane transport
A	0016020	cellular_component	membrane
A	0042802	molecular_function	identical protein binding
A	0051475	biological_process	glucosylglycerol transmembrane transport
A	0055085	biological_process	transmembrane transport
A	0071918	biological_process	urea transmembrane transport
A	0072488	biological_process	ammonium transmembrane transport

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	120
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	62
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	34
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18500352","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3C02","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---