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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7S9B

Cryo-EM Structure of dolphin Prestin: Sensor Down I (Expanded) state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005886	cellular_component	plasma membrane
A	0007605	biological_process	sensory perception of sound
A	0008271	molecular_function	secondary active sulfate transmembrane transporter activity
A	0008360	biological_process	regulation of cell shape
A	0016020	cellular_component	membrane
A	0055085	biological_process	transmembrane transport
A	0099129	biological_process	cochlear outer hair cell electromotile response
A	1902358	biological_process	sulfate transmembrane transport
B	0005886	cellular_component	plasma membrane
B	0007605	biological_process	sensory perception of sound
B	0008271	molecular_function	secondary active sulfate transmembrane transporter activity
B	0008360	biological_process	regulation of cell shape
B	0016020	cellular_component	membrane
B	0055085	biological_process	transmembrane transport
B	0099129	biological_process	cochlear outer hair cell electromotile response
B	1902358	biological_process	sulfate transmembrane transport

Functional Information from PROSITE/UniProt

site_id	PS01130
Number of Residues	22
Details	SLC26A SLC26A transporters signature. PvFGLYSSfypvIMYcffGTSR

Chain	Residue	Details
A	PRO109-ARG130

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	640
Details	TOPO_DOM: Cytoplasmic => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	MET1-TYR79
A	VAL499-ALA741
B	MET1-TYR79
B	VAL499-ALA741

site_id	SWS_FT_FI2
Number of Residues	50
Details	TRANSMEM: Helical; Name=1 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	VAL80-ALA105
B	VAL80-ALA105

site_id	SWS_FT_FI3
Number of Residues	210
Details	TOPO_DOM: Extracellular => ECO:0000305\|PubMed:34695838

Chain	Residue	Details
A	ALA106-PRO109
B	ALA148-VAL178
B	GLY231-VAL243
B	ALA249-SER261
B	SER304-LEU338
B	GLN389-SER396
B	PHE430-PRO436
B	LEU484
A	ALA148-VAL178
A	GLY231-VAL243
A	ALA249-SER261
A	SER304-LEU338
A	GLN389-SER396
A	PHE430-PRO436
A	LEU484
B	ALA106-PRO109

site_id	SWS_FT_FI4
Number of Residues	30
Details	TRANSMEM: Helical; Name=2 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	VAL110-PHE125
B	VAL110-PHE125

site_id	SWS_FT_FI5
Number of Residues	72
Details	TOPO_DOM: Cytoplasmic => ECO:0000305\|PubMed:34695838

Chain	Residue	Details
A	PHE126-PHE137
B	PHE460-ILE467
A	GLU284-PRO291
A	ALA362-ASP370
A	GLY407-THR410
A	PHE460-ILE467
B	PHE126-PHE137
B	GLU284-PRO291
B	ALA362-ASP370
B	GLY407-THR410

site_id	SWS_FT_FI6
Number of Residues	18
Details	TRANSMEM: Helical; Name=3 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	ALA138-VAL147
B	ALA138-VAL147

site_id	SWS_FT_FI7
Number of Residues	58
Details	TRANSMEM: Helical; Name=4 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	ALA179-PRO208
B	ALA179-PRO208

site_id	SWS_FT_FI8
Number of Residues	42
Details	TRANSMEM: Helical; Name=5a => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	LEU209-PHE230
B	LEU209-PHE230

site_id	SWS_FT_FI9
Number of Residues	8
Details	INTRAMEM: Helical; Name=5b => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	VAL244-VAL248
B	VAL244-VAL248

site_id	SWS_FT_FI10
Number of Residues	42
Details	TRANSMEM: Helical; Name=6 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	LEU262-LYS283
B	LEU262-LYS283

site_id	SWS_FT_FI11
Number of Residues	22
Details	TRANSMEM: Helical; Name=7 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	LEU292-ILE303
B	LEU292-ILE303

site_id	SWS_FT_FI12
Number of Residues	44
Details	TRANSMEM: Helical; Name=8 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	VAL339-LEU361
B	VAL339-LEU361

site_id	SWS_FT_FI13
Number of Residues	34
Details	TRANSMEM: Helical; Name=9 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	GLY371-PHE388
B	GLY371-PHE388

site_id	SWS_FT_FI14
Number of Residues	18
Details	TRANSMEM: Helical; Name=10 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	LEU397-THR406
B	LEU397-THR406

site_id	SWS_FT_FI15
Number of Residues	36
Details	TRANSMEM: Helical; Name=11 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	GLN411-GLY429
B	GLN411-GLY429

site_id	SWS_FT_FI16
Number of Residues	44
Details	TRANSMEM: Helical; Name=12 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	GLN437-PRO459
B	GLN437-PRO459

site_id	SWS_FT_FI17
Number of Residues	30
Details	TRANSMEM: Helical; Name=13 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	GLU468-GLY483
B	GLU468-GLY483

site_id	SWS_FT_FI18
Number of Residues	26
Details	TRANSMEM: Helical; Name=14 => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S8X

Chain	Residue	Details
A	ASP485-THR498
B	ASP485-THR498

site_id	SWS_FT_FI19
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:34695838, ECO:0007744\|PDB:7S9E

Chain	Residue	Details
A	SER398
B	SER398

site_id	SWS_FT_FI20
Number of Residues	2
Details	SITE: Controls the electromotile activity => ECO:0000250\|UniProtKB:A0FKN5, ECO:0000250\|UniProtKB:Q9EPH0

Chain	Residue	Details
A	SER398
B	SER398

site_id	SWS_FT_FI21
Number of Residues	2
Details	SITE: Contributes to anion binding => ECO:0000250\|UniProtKB:Q9EPH0

Chain	Residue	Details
A	ARG399
B	ARG399

site_id	SWS_FT_FI22
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN163
A	ASN166
B	ASN163
B	ASN166

227111

PDB entries from 2024-11-06

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