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2V8N

Wild-type Structure of Lactose Permease

Functional Information from GO Data
ChainGOidnamespacecontents
A0005351molecular_functioncarbohydrate:proton symporter activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008643biological_processcarbohydrate transport
A0015212molecular_functioncytidine transmembrane transporter activity
A0015213molecular_functionuridine transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015528molecular_functionlactose:proton symporter activity
A0015767biological_processlactose transport
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0030395molecular_functionlactose binding
A0034219biological_processcarbohydrate transmembrane transport
A0055085biological_processtransmembrane transport
A0071702biological_processorganic substance transport
A1902600biological_processproton transmembrane transport
B0005351molecular_functioncarbohydrate:proton symporter activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008643biological_processcarbohydrate transport
B0015212molecular_functioncytidine transmembrane transporter activity
B0015213molecular_functionuridine transmembrane transporter activity
B0015293molecular_functionsymporter activity
B0015528molecular_functionlactose:proton symporter activity
B0015767biological_processlactose transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0030395molecular_functionlactose binding
B0034219biological_processcarbohydrate transmembrane transport
B0055085biological_processtransmembrane transport
B0071702biological_processorganic substance transport
B1902600biological_processproton transmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00896
Number of Residues15
DetailsLACY_1 LacY family proton/sugar symporters signature 1. GLLsDKLGLRKyLLW
ChainResidueDetails
AGLY64-TRP78

site_idPS00897
Number of Residues15
DetailsLACY_2 LacY family proton/sugar symporters signature 2. PlIINRIGgKNALLL
ChainResidueDetails
APRO280-LEU294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues144
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:2164211
ChainResidueDetails
AMET1-THR7
BALA187-PRO220
BALA279-GLY288
BLYS335-SER346
AGLY71-LYS74
AGLU130-PHE140
AALA187-PRO220
AALA279-GLY288
ALYS335-SER346
BMET1-THR7
BGLY71-LYS74
BGLU130-PHE140

site_idSWS_FT_FI2
Number of Residues52
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AASN8-LEU34
BASN8-LEU34

site_idSWS_FT_FI3
Number of Residues36
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:2164211
ChainResidueDetails
AHIS35-SER41
BPHE250-THR253
BALA309-SER311
BSER375-GLY377
ATYR101-LEU104
AILE164-ASN166
APHE250-THR253
AALA309-SER311
ASER375-GLY377
BHIS35-SER41
BTYR101-LEU104
BILE164-ASN166

site_idSWS_FT_FI4
Number of Residues56
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ALYS42-LEU70
BLYS42-LEU70

site_idSWS_FT_FI5
Number of Residues50
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ATYR75-GLN100
BTYR75-GLN100

site_idSWS_FT_FI6
Number of Residues48
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AVAL105-ILE129
BVAL105-ILE129

site_idSWS_FT_FI7
Number of Residues44
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLY141-THR163
BGLY141-THR163

site_idSWS_FT_FI8
Number of Residues38
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AGLN167-PHE186
BGLN167-PHE186

site_idSWS_FT_FI9
Number of Residues56
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
ALYS221-SER249
BLYS221-SER249

site_idSWS_FT_FI10
Number of Residues48
DetailsTRANSMEM: Helical; Name=8
ChainResidueDetails
AGLY254-PHE278
BGLY254-PHE278

site_idSWS_FT_FI11
Number of Residues38
DetailsTRANSMEM: Helical; Name=9
ChainResidueDetails
ALYS289-PHE308
BLYS289-PHE308

site_idSWS_FT_FI12
Number of Residues44
DetailsTRANSMEM: Helical; Name=10
ChainResidueDetails
AALA312-PHE334
BALA312-PHE334

site_idSWS_FT_FI13
Number of Residues54
DetailsTRANSMEM: Helical; Name=11
ChainResidueDetails
AALA347-GLU374
BALA347-GLU374

site_idSWS_FT_FI14
Number of Residues40
DetailsTRANSMEM: Helical; Name=12
ChainResidueDetails
APHE378-PHE398
BPHE378-PHE398

site_idSWS_FT_FI15
Number of Residues36
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2164211
ChainResidueDetails
ATHR399-ALA417
BTHR399-ALA417

site_idSWS_FT_FI16
Number of Residues4
DetailsSITE: Substrate binding => ECO:0000305|PubMed:12893935
ChainResidueDetails
AGLU126
AARG144
BGLU126
BARG144

site_idSWS_FT_FI17
Number of Residues2
DetailsSITE: Substrate binding and proton translocation => ECO:0000305|PubMed:12893935
ChainResidueDetails
AGLU269
BGLU269

site_idSWS_FT_FI18
Number of Residues6
DetailsSITE: Proton translocation => ECO:0000305|PubMed:12893935
ChainResidueDetails
AARG302
AHIS322
AGLU325
BARG302
BHIS322
BGLU325

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N-formylmethionine; partial => ECO:0000269|PubMed:10485888
ChainResidueDetails
AMET1
BMET1

218853

PDB entries from 2024-04-24

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