4NEF

X-ray structure of human Aquaporin 2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015267	molecular_function	channel activity
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
B	0015267	molecular_function	channel activity
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
C	0015267	molecular_function	channel activity
C	0016020	cellular_component	membrane
C	0055085	biological_process	transmembrane transport
D	0015267	molecular_function	channel activity
D	0016020	cellular_component	membrane
D	0055085	biological_process	transmembrane transport

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD A 301

Chain	Residue
A	GLU155
A	HOH405
D	GLN57
D	HOH409

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ZN A 302

Chain	Residue
A	CYS75
A	HIS80
A	HOH413

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD D 301

Chain	Residue
C	HIS80
C	GLU232

---

Functional Information from PROSITE/UniProt

site_id	PS00221
Number of Residues	9
Details	MIP MIP family signature. HINPAVTVA

Chain	Residue	Details
A	HIS66-ALA74

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	472
Details	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	144
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	84
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	84
Details	Intramembrane: {"description":"Discontinuously helical","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NEF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Motif: {"description":"NPA 1","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	Motif: {"description":"NPA 2","evidences":[{"source":"PubMed","id":"24733887","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---