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2CFQ

Sugar Free Lactose Permease at neutral pH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005351molecular_functioncarbohydrate:proton symporter activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008643biological_processcarbohydrate transport
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
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 501
ChainResidue
ACYS148
AGLU269

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 502
ChainResidue
APHE21
AGLY173
ACYS176
AALA177

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 503
ChainResidue
APHE356
ALEU57
APRO61
ACYS355

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 504
ChainResidue
ACYS333
ATYR350
APHE354

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 505
ChainResidue
AILE230
ACYS234
ATHR235
AMET365

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 Residues72
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:2164211
ChainResidueDetails
AMET1-THR7
AGLY71-LYS74
AGLU130-PHE140
AALA187-PRO220
AALA279-GLY288
ALYS335-SER346

site_idSWS_FT_FI2
Number of Residues26
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
AASN8-LEU34

site_idSWS_FT_FI3
Number of Residues18
DetailsTOPO_DOM: Periplasmic => ECO:0000269|PubMed:2164211
ChainResidueDetails
AHIS35-SER41
ATYR101-LEU104
AILE164-ASN166
APHE250-THR253
AALA309-SER311
ASER375-GLY377

site_idSWS_FT_FI4
Number of Residues28
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ALYS42-LEU70

site_idSWS_FT_FI5
Number of Residues25
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
ATYR75-GLN100

site_idSWS_FT_FI6
Number of Residues24
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AVAL105-ILE129

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
AGLY141-THR163

site_idSWS_FT_FI8
Number of Residues19
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
AGLN167-PHE186

site_idSWS_FT_FI9
Number of Residues28
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
ALYS221-SER249

site_idSWS_FT_FI10
Number of Residues24
DetailsTRANSMEM: Helical; Name=8
ChainResidueDetails
AGLY254-PHE278

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=9
ChainResidueDetails
ALYS289-PHE308

site_idSWS_FT_FI12
Number of Residues22
DetailsTRANSMEM: Helical; Name=10
ChainResidueDetails
AALA312-PHE334

site_idSWS_FT_FI13
Number of Residues27
DetailsTRANSMEM: Helical; Name=11
ChainResidueDetails
AALA347-GLU374

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12
ChainResidueDetails
APHE378-PHE398

site_idSWS_FT_FI15
Number of Residues18
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2164211
ChainResidueDetails
ATHR399-ALA417

site_idSWS_FT_FI16
Number of Residues2
DetailsSITE: Substrate binding => ECO:0000305|PubMed:12893935
ChainResidueDetails
AGLU126
AARG144

site_idSWS_FT_FI17
Number of Residues1
DetailsSITE: Substrate binding and proton translocation => ECO:0000305|PubMed:12893935
ChainResidueDetails
AGLU269

site_idSWS_FT_FI18
Number of Residues3
DetailsSITE: Proton translocation => ECO:0000305|PubMed:12893935
ChainResidueDetails
AARG302
AHIS322
AGLU325

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: N-formylmethionine; partial => ECO:0000269|PubMed:10485888
ChainResidueDetails
AMET1

219140

PDB entries from 2024-05-01

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