5MJU

Structure of the thermostabilized EAAT1 cryst mutant in complex with the competititve inhibitor TFB-TBOA and the allosteric inhibitor UCPH101

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0015293	molecular_function	symporter activity
A	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	binding site for residue 6Z6 A 601

Chain	Residue
A	SER116
A	GLY117
A	VAL124
A	TYR127
A	MET231
A	PHE235
A	PHE369
A	VAL373

---

site_id	AC2
Number of Residues	22
Details	binding site for residue 7O9 A 602

Chain	Residue
A	ILE100
A	ILE223
A	SER343
A	SER344
A	SER345
A	SER346
A	LEU349
A	PRO372
A	ALA375
A	THR376
A	MET379
A	THR382
A	GLY419
A	ALA420
A	GLN425
A	ALA426
A	GLY427
A	ASP456
A	ARG459
A	THR460
A	ASN463
A	ILE96

---

Functional Information from PROSITE/UniProt

site_id	PS00713
Number of Residues	15
Details	NA_DICARBOXYL_SYMP_1 Sodium:dicarboxylate symporter family signature 1. P.GElLMrMLKMLIlP

Chain	Residue	Details
A	PRO84-PRO98

---

site_id	PS00714
Number of Residues	24
Details	NA_DICARBOXYL_SYMP_2 Sodium:dicarboxylate symporter family signature 2. PvGaTiNMDGTaLYeaVaaIFIAQ

Chain	Residue	Details
A	PRO372-GLN395

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	122
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	MET1-ARG47
A	ALA109-ARG122
A	GLY241-ASP249
A	GLU357-ARG365
A	GLU475-MET522

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	TRANSMEM: Helical; Name=1 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	ASN48-LEU68

---

site_id	SWS_FT_FI3
Number of Residues	61
Details	TOPO_DOM: Extracellular => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	ARG69-GLU86
A	ALA278-MET298
A	ILE393-GLN405
A	LEU440-ASP452

---

site_id	SWS_FT_FI4
Number of Residues	21
Details	TRANSMEM: Helical; Name=2 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	LEU87-LEU108

---

site_id	SWS_FT_FI5
Number of Residues	22
Details	TRANSMEM: Helical; Name=3 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	ALA123-ILE145

---

site_id	SWS_FT_FI6
Number of Residues	27
Details	TRANSMEM: Helical; Name=5 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	PHE250-ILE277

---

site_id	SWS_FT_FI7
Number of Residues	21
Details	TRANSMEM: Helical; Name=6 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	VAL299-ILE320

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	TOPO_DOM: Cytoplasmic => ECO:0000305

Chain	Residue	Details
A	THR321-PRO325

---

site_id	SWS_FT_FI9
Number of Residues	63
Details	INTRAMEM: Discontinuously helical => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	PHE326-LEU356
A	ILE406-GLY439

---

site_id	SWS_FT_FI10
Number of Residues	26
Details	TRANSMEM: Helical; Name=7 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	ILE366-PHE392

---

site_id	SWS_FT_FI11
Number of Residues	21
Details	TRANSMEM: Helical; Name=8 => ECO:0000305|PubMed:28424515

Chain	Residue	Details
A	TRP453-VAL474

---

site_id	SWS_FT_FI12
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:28424515, ECO:0007744|PDB:5LM4

Chain	Residue	Details
A	SER343
A	THR376
A	THR382
A	ILE423
A	ASP456

---

site_id	SWS_FT_FI13
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:O59010

Chain	Residue	Details
A	GLY374
A	ASN378
A	ASN463
A	ASP467

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER492

---

site_id	SWS_FT_FI15
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	THR155

---

site_id	SWS_FT_FI16
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973

Chain	Residue	Details
A	THR204

---