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3GD8

Crystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of Conductance

Functional Information from GO Data
ChainGOidnamespacecontents
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00221
Number of Residues9
DetailsMIP MIP family signature. HINPAVTVA
ChainResidueDetails
AHIS95-ALA103

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues119
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:19383790
ChainResidueDetails
AALA37-ILE57
AMET70-GLY89
AVAL116-VAL136
AALA156-ALA176
AVAL185-ILE205
AILE232-PHE252

site_idSWS_FT_FI2
Number of Residues39
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:19383790
ChainResidueDetails
AASN58-ASP69
ATHR137-THR155
AASN206-THR208
AILE223-TRP231

site_idSWS_FT_FI3
Number of Residues23
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:19383790
ChainResidueDetails
AHIS90-GLY93
AVAL102-SER115
ASER177-ASP184

site_idSWS_FT_FI4
Number of Residues20
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:19383790
ChainResidueDetails
AGLY94-THR101
AGLY209-VAL222

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKG => ECO:0000250|UniProtKB:P55088
ChainResidueDetails
ASER111

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:P47863
ChainResidueDetails
ASER180

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153
AASN206

224201

PDB entries from 2024-08-28

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