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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 Residues17
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
APHE37-SER54

site_idSWS_FT_FI2
Number of Residues69
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:36737436
ChainResidueDetails
AVAL55-TYR67
ALEU133-ARG170
AGLY218-THR221
APHE236-TRP253

site_idSWS_FT_FI3
Number of Residues17
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
ALEU68-ALA85

site_idSWS_FT_FI4
Number of Residues21
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:36737436
ChainResidueDetails
AGLY86-SER89
ALEU104-LYS111
AILE189-GLY200

site_idSWS_FT_FI5
Number of Residues26
DetailsINTRAMEM: Discontinuously helical => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
AGLY90-ALA103
AGLY222-ILE235

site_idSWS_FT_FI6
Number of Residues20
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
APHE112-SER132

site_idSWS_FT_FI7
Number of Residues17
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
AGLY171-ALA188

site_idSWS_FT_FI8
Number of Residues16
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
ATHR201-LEU217

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:36737436, ECO:0007744|PDB:8AMW, ECO:0007744|PDB:8AMX
ChainResidueDetails
ATRP254-PHE275

site_idSWS_FT_FI10
Number of Residues3
DetailsSITE: Selectivity filter => ECO:0000305|PubMed:36737436
ChainResidueDetails
APHE74
ATYR223
AARG229

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Important for permeability to glycerol => ECO:0000269|PubMed:30423801
ChainResidueDetails
ATYR135

229183

PDB entries from 2024-12-18

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