Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7LH2

Structure of human prestin in the presence of sodium salicylate and sodium sulfate

Functional Information from GO Data
ChainGOidnamespacecontents
A0002931biological_processresponse to ischemia
A0005886cellular_componentplasma membrane
A0006821biological_processchloride transport
A0007605biological_processsensory perception of sound
A0008271molecular_functionsecondary active sulfate transmembrane transporter activity
A0008272biological_processsulfate transport
A0008360biological_processregulation of cell shape
A0009410biological_processresponse to xenobiotic stimulus
A0009751biological_processresponse to salicylic acid
A0010996biological_processresponse to auditory stimulus
A0015106molecular_functionbicarbonate transmembrane transporter activity
A0015108molecular_functionchloride transmembrane transporter activity
A0015116molecular_functionsulfate transmembrane transporter activity
A0015701biological_processbicarbonate transport
A0015755biological_processfructose transmembrane transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016328cellular_componentlateral plasma membrane
A0019531molecular_functionoxalate transmembrane transporter activity
A0019532biological_processoxalate transport
A0030507molecular_functionspectrin binding
A0034220biological_processmonoatomic ion transmembrane transport
A0034766biological_processnegative regulation of monoatomic ion transmembrane transport
A0035864biological_processresponse to potassium ion
A0042391biological_processregulation of membrane potential
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0045793biological_processpositive regulation of cell size
A0055085biological_processtransmembrane transport
A0090102biological_processcochlea development
A0097066biological_processresponse to thyroid hormone
A0098656biological_processmonoatomic anion transmembrane transport
A0120249cellular_componentlateral wall of outer hair cell
A0140900molecular_functionchloride:bicarbonate antiporter activity
A1902074biological_processresponse to salt
A1902358biological_processsulfate transmembrane transport
A1902476biological_processchloride transmembrane transport
A2000147biological_processpositive regulation of cell motility
B0002931biological_processresponse to ischemia
B0005886cellular_componentplasma membrane
B0006821biological_processchloride transport
B0007605biological_processsensory perception of sound
B0008271molecular_functionsecondary active sulfate transmembrane transporter activity
B0008272biological_processsulfate transport
B0008360biological_processregulation of cell shape
B0009410biological_processresponse to xenobiotic stimulus
B0009751biological_processresponse to salicylic acid
B0010996biological_processresponse to auditory stimulus
B0015106molecular_functionbicarbonate transmembrane transporter activity
B0015108molecular_functionchloride transmembrane transporter activity
B0015116molecular_functionsulfate transmembrane transporter activity
B0015701biological_processbicarbonate transport
B0015755biological_processfructose transmembrane transport
B0016020cellular_componentmembrane
B0016323cellular_componentbasolateral plasma membrane
B0016328cellular_componentlateral plasma membrane
B0019531molecular_functionoxalate transmembrane transporter activity
B0019532biological_processoxalate transport
B0030507molecular_functionspectrin binding
B0034220biological_processmonoatomic ion transmembrane transport
B0034766biological_processnegative regulation of monoatomic ion transmembrane transport
B0035864biological_processresponse to potassium ion
B0042391biological_processregulation of membrane potential
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0045793biological_processpositive regulation of cell size
B0055085biological_processtransmembrane transport
B0090102biological_processcochlea development
B0097066biological_processresponse to thyroid hormone
B0098656biological_processmonoatomic anion transmembrane transport
B0120249cellular_componentlateral wall of outer hair cell
B0140900molecular_functionchloride:bicarbonate antiporter activity
B1902074biological_processresponse to salt
B1902358biological_processsulfate transmembrane transport
B1902476biological_processchloride transmembrane transport
B2000147biological_processpositive regulation of cell motility
Functional Information from PROSITE/UniProt
site_idPS01130
Number of Residues22
DetailsSLC26A SLC26A transporters signature. PiFGLYSSfypvIMYcflGTSR
ChainResidueDetails
APRO109-ARG130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues692
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-LYS75
BGLY127-PHE137
BARG197-THR206
BLYS283-PRO291
BGLN368-ASP370
BGLY407-THR410
BSER465
BSER505-ALA744
AGLY127-PHE137
AARG197-THR206
ALYS283-PRO291
AGLN368-ASP370
AGLY407-THR410
ASER465
ASER505-ALA744
BMET1-LYS75

site_idSWS_FT_FI2
Number of Residues58
DetailsTRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
APHE76-ALA105
BPHE76-ALA105

site_idSWS_FT_FI3
Number of Residues134
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AALA106-PRO108
BVAL152-THR168
BGLY231-PHE241
BVAL254-ASN258
BASN308-ASP332
BGLN389-SER396
BGLU433-PRO436
BLEU482-GLY483
AVAL152-THR168
AGLY231-PHE241
AVAL254-ASN258
AASN308-ASP332
AGLN389-SER396
AGLU433-PRO436
ALEU482-GLY483
BALA106-PRO108

site_idSWS_FT_FI4
Number of Residues34
DetailsTRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
APRO109-LEU126
BPRO109-LEU126

site_idSWS_FT_FI5
Number of Residues26
DetailsTRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AALA138-LEU151
BALA138-LEU151

site_idSWS_FT_FI6
Number of Residues54
DetailsTRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AGLU169-CYS196
BGLU169-CYS196

site_idSWS_FT_FI7
Number of Residues46
DetailsTRANSMEM: Helical; Name=5a => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AGLU207-PHE230
BGLU207-PHE230

site_idSWS_FT_FI8
Number of Residues22
DetailsINTRAMEM: Helical; Name=5b => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ASER242-ASN253
BSER242-ASN253

site_idSWS_FT_FI9
Number of Residues46
DetailsTRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AVAL259-PHE282
BVAL259-PHE282

site_idSWS_FT_FI10
Number of Residues30
DetailsTRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ALEU292-PHE307
BLEU292-PHE307

site_idSWS_FT_FI11
Number of Residues68
DetailsTRANSMEM: Helical; Name=8 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ATHR333-TYR367
BTHR333-TYR367

site_idSWS_FT_FI12
Number of Residues34
DetailsTRANSMEM: Helical; Name=9 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AGLY371-PHE388
BGLY371-PHE388

site_idSWS_FT_FI13
Number of Residues18
DetailsTRANSMEM: Helical; Name=10 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ALEU397-THR406
BLEU397-THR406

site_idSWS_FT_FI14
Number of Residues42
DetailsTRANSMEM: Helical; Name=11 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AGLN411-PHE432
BGLN411-PHE432

site_idSWS_FT_FI15
Number of Residues54
DetailsTRANSMEM: Helical; Name=12 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
AGLN437-THR464
BGLN437-THR464

site_idSWS_FT_FI16
Number of Residues30
DetailsTRANSMEM: Helical; Name=13 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ALYS466-PHE481
BLYS466-PHE481

site_idSWS_FT_FI17
Number of Residues40
DetailsTRANSMEM: Helical; Name=14 => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LGU, ECO:0007744|PDB:7LGW, ECO:0007744|PDB:7LH2, ECO:0007744|PDB:7LH3
ChainResidueDetails
ALEU484-GLN504
BLEU484-GLN504

site_idSWS_FT_FI18
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:34390643, ECO:0007744|PDB:7LH2
ChainResidueDetails
ASER398
BSER398

site_idSWS_FT_FI19
Number of Residues2
DetailsSITE: Controls the electromotile activity => ECO:0000250|UniProtKB:A0FKN5, ECO:0000250|UniProtKB:Q9EPH0
ChainResidueDetails
ASER398
BSER398

site_idSWS_FT_FI20
Number of Residues2
DetailsSITE: Contributes to anion binding => ECO:0000250|UniProtKB:Q9EPH0
ChainResidueDetails
AARG399
BARG399

site_idSWS_FT_FI21
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN163
AASN166
BASN163
BASN166

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon