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3NKA

Crystal structure of AqpZ H174G,T183F

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006833biological_processwater transport
A0006970biological_processresponse to osmotic stress
A0009992biological_processintracellular water homeostasis
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0055085biological_processtransmembrane transport
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006833biological_processwater transport
B0006970biological_processresponse to osmotic stress
B0009992biological_processintracellular water homeostasis
B0015250molecular_functionwater channel activity
B0015267molecular_functionchannel activity
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HFNPAVTIG
ChainResidueDetails
AHIS61-GLY69

site_idPS00501
Number of Residues8
DetailsSPASE_I_1 Signal peptidases I serine active site. GYSMLSAL
ChainResidueDetails
AGLY128-LEU135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues108
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues40
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsMotif: {"description":"NPA 1"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsMotif: {"description":"NPA 2"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsSite: {"description":"Involved in tetramerization or stability of the tetramer"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues8
DetailsSite: {"description":"Selectivity filter"}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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