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5LLU

Structure of the thermostabilized EAAT1 cryst-II mutant in complex with L-ASP

Functional Information from GO Data
ChainGOidnamespacecontents
A0015293molecular_functionsymporter activity
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue NA A 601
ChainResidue
ATHR376
AILE377
AMET379
ASER417
AILE418
AALA420

site_idAC2
Number of Residues14
Detailsbinding site for residue ASP A 602
ChainResidue
ATHR382
AALA421
AGLY422
AILE423
AGLN425
AALA426
AGLY427
AASP456
AARG459
ATHR460
AASN463
ASER343
ASER344
ASER345

Functional Information from PROSITE/UniProt
site_idPS00713
Number of Residues15
DetailsNA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GElLMrMLKMLIlP
ChainResidueDetails
APRO84-PRO98

site_idPS00714
Number of Residues24
DetailsNA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PvGaTiNMDGTaLYeaVaaIFIAQ
ChainResidueDetails
APRO372-GLN395

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues122
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:28424515
ChainResidueDetails
AMET1-ARG47
AALA109-ARG122
AGLY241-ASP249
AGLU357-ARG365
AGLU475-MET522

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical; Name=1 => ECO:0000305|PubMed:28424515
ChainResidueDetails
AASN48-LEU68

site_idSWS_FT_FI3
Number of Residues61
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:28424515
ChainResidueDetails
AARG69-GLU86
AALA278-MET298
AILE393-GLN405
ALEU440-ASP452

site_idSWS_FT_FI4
Number of Residues21
DetailsTRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:28424515
ChainResidueDetails
ALEU87-LEU108

site_idSWS_FT_FI5
Number of Residues22
DetailsTRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:28424515
ChainResidueDetails
AALA123-ILE145

site_idSWS_FT_FI6
Number of Residues27
DetailsTRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:28424515
ChainResidueDetails
APHE250-ILE277

site_idSWS_FT_FI7
Number of Residues21
DetailsTRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:28424515
ChainResidueDetails
AVAL299-ILE320

site_idSWS_FT_FI8
Number of Residues4
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
ATHR321-PRO325

site_idSWS_FT_FI9
Number of Residues63
DetailsINTRAMEM: Discontinuously helical => ECO:0000305|PubMed:28424515
ChainResidueDetails
APHE326-LEU356
AILE406-GLY439

site_idSWS_FT_FI10
Number of Residues26
DetailsTRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:28424515
ChainResidueDetails
AILE366-PHE392

site_idSWS_FT_FI11
Number of Residues21
DetailsTRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:28424515
ChainResidueDetails
ATRP453-VAL474

site_idSWS_FT_FI12
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:28424515, ECO:0007744|PDB:5LM4
ChainResidueDetails
ASER343
ATHR376
ATHR382
AILE423
AASP456

site_idSWS_FT_FI13
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O59010
ChainResidueDetails
AGLY374
AASN378
AASN463
AASP467

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER492

site_idSWS_FT_FI15
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATHR155

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
ATHR204

226707

PDB entries from 2024-10-30

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