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2D57

Double layered 2D crystal structure of AQUAPORIN-4 (AQP4M23) at 3.2 a resolution by electron crystallography

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0006833biological_processwater transport
A0007565biological_processfemale pregnancy
A0007605biological_processsensory perception of sound
A0009897cellular_componentexternal side of plasma membrane
A0009925cellular_componentbasal plasma membrane
A0009992biological_processintracellular water homeostasis
A0010008cellular_componentendosome membrane
A0010574biological_processregulation of vascular endothelial growth factor production
A0015250molecular_functionwater channel activity
A0015267molecular_functionchannel activity
A0015670biological_processcarbon dioxide transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0030315cellular_componentT-tubule
A0031253cellular_componentcell projection membrane
A0032691biological_processnegative regulation of interleukin-1 beta production
A0032715biological_processnegative regulation of interleukin-6 production
A0032991cellular_componentprotein-containing complex
A0033326biological_processcerebrospinal fluid secretion
A0042383cellular_componentsarcolemma
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0050891biological_processmulticellular organismal-level water homeostasis
A0051289biological_processprotein homotetramerization
A0051384biological_processresponse to glucocorticoid
A0051649biological_processestablishment of localization in cell
A0055085biological_processtransmembrane transport
A0060354biological_processnegative regulation of cell adhesion molecule production
A0070295biological_processrenal water absorption
A0071333biological_processcellular response to glucose stimulus
A0071346biological_processcellular response to type II interferon
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0071392biological_processcellular response to estradiol stimulus
A0090660biological_processcerebrospinal fluid circulation
A0097450cellular_componentastrocyte end-foot
A0098609biological_processcell-cell adhesion
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:16325200, ECO:0000269|PubMed:19406128
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:16325200, ECO:0000269|PubMed:19406128
ChainResidueDetails
AASN58-ASP69
ATHR137-THR155
AASN206-THR208
AILE223-TRP231

site_idSWS_FT_FI3
Number of Residues93
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:16325200, ECO:0000269|PubMed:19406128
ChainResidueDetails
AHIS90-GLY93
AVAL102-SER115
ASER177-ASP184
ACYS253-VAL323

site_idSWS_FT_FI4
Number of Residues20
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:16325200, ECO:0000269|PubMed:19406128
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:0000269|PubMed:19800950
ChainResidueDetails
ASER180

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER276

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12692561, ECO:0007744|PubMed:22673903
ChainResidueDetails
ASER285

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P55088
ChainResidueDetails
ATHR289

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16641100
ChainResidueDetails
ASER321

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN153

219869

PDB entries from 2024-05-15

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