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6QZI

Crystal structure of human Aquaporin 7 at 1.9 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0015267molecular_functionchannel activity
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 301
ChainResidue
AGLY86
AGLY90
AASN195
AGLU202
AHOH402

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 302
ChainResidue
AARG229
AGOL308
AGOL312
AHOH405
APHE74
AGLY222
ATYR223
AALA224

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 303
ChainResidue
ALEU60
AASN61
AALA137
AHIS140
AHIS165
AMET219

site_idAC4
Number of Residues4
Detailsbinding site for residue GOL A 304
ChainResidue
AALA103
ATRP109
ATHR149
AHOH406

site_idAC5
Number of Residues4
Detailsbinding site for residue GOL A 305
ChainResidue
AARG35
AGLU193
AILE276
ATHR279

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL A 306
ChainResidue
AGLY156
AALA159
ATHR160
ATYR161
AGOL308
AHOH425

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL A 307
ChainResidue
AMET58
AVAL59
AASN61
ALYS62
APHE141
AHOH417

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL A 308
ChainResidue
AVAL55
AVAL70
AGLY222
AARG229
AGOL302
AGOL306
AHOH403

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL A 309
ChainResidue
ALYS62
AGLY65
ASER66
ASER66
ATYR67
ALEU68
AHOH416

site_idAD1
Number of Residues3
Detailsbinding site for residue GOL A 310
ChainResidue
ASER132
ATYR135
AARG170

site_idAD2
Number of Residues3
Detailsbinding site for residue GOL A 311
ChainResidue
AARG106
ATHR190
AASP191

site_idAD3
Number of Residues9
Detailsbinding site for residue GOL A 312
ChainResidue
AVAL78
AHIS92
AASN94
AASN226
AGOL302
AGOL313
AHOH401
AHOH404
AHOH405

site_idAD4
Number of Residues10
Detailsbinding site for residue GOL A 313
ChainResidue
AALA91
AHIS92
AMET93
AASN94
ALEU182
ALEU186
AGOL312
AHOH401
AHOH404
AHOH434

site_idAD5
Number of Residues3
Detailsbinding site for residue GOL A 314
ChainResidue
AARG110
AHIS140
AHIS165

site_idAD6
Number of Residues5
Detailsbinding site for residue PO4 A 315
ChainResidue
ALEU146
AGLY241
ATRP242
AGLY243
AGLN245

site_idAD7
Number of Residues3
Detailsbinding site for residue PO4 A 316
ChainResidue
ALEU198
AGLY200
AHOH428

site_idAD8
Number of Residues2
Detailsbinding site for residue PO4 A 317
ChainResidue
APHE247
AASN252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues115
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:P55087
ChainResidueDetails
AGLU36-ALA56
ATYR67-GLY86
APRO113-VAL148
ALEU168-ALA188
ALEU198-MET219

site_idSWS_FT_FI2
Number of Residues28
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AHIS57-SER66
ATHR149-THR167
AASN220-THR221

site_idSWS_FT_FI3
Number of Residues24
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AARG87-GLY90
APHE99-PHE112
AILE189-ALA197

site_idSWS_FT_FI4
Number of Residues20
DetailsINTRAMEM: Discontinuously helical => ECO:0000250|UniProtKB:P55087
ChainResidueDetails
AALA91-THR98
AGLY222-ILE235

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for permeability to glycerol => ECO:0000269|PubMed:30423801
ChainResidueDetails
ATYR135

226707

PDB entries from 2024-10-30

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