Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5EQH

Human GLUT1 in complex with inhibitor (2~{S})-3-(2-bromophenyl)-2-[2-(4-methoxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0001666biological_processresponse to hypoxia
A0001674cellular_componentfemale germ cell nucleus
A0001917cellular_componentphotoreceptor inner segment
A0001939cellular_componentfemale pronucleus
A0005324molecular_functionlong-chain fatty acid transmembrane transporter activity
A0005355molecular_functionglucose transmembrane transporter activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
A0005911cellular_componentcell-cell junction
A0007417biological_processcentral nervous system development
A0007565biological_processfemale pregnancy
A0014704cellular_componentintercalated disc
A0015911biological_processlong-chain fatty acid import across plasma membrane
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0019852biological_processL-ascorbic acid metabolic process
A0019900molecular_functionkinase binding
A0021987biological_processcerebral cortex development
A0022857molecular_functiontransmembrane transporter activity
A0030018cellular_componentZ disc
A0030496cellular_componentmidbody
A0030864cellular_componentcortical actin cytoskeleton
A0031982cellular_componentvesicle
A0032868biological_processresponse to insulin
A0033300molecular_functiondehydroascorbic acid transmembrane transporter activity
A0042149biological_processcellular response to glucose starvation
A0042383cellular_componentsarcolemma
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042908biological_processxenobiotic transport
A0042910molecular_functionxenobiotic transmembrane transporter activity
A0045121cellular_componentmembrane raft
A0045202cellular_componentsynapse
A0045494biological_processphotoreceptor cell maintenance
A0046323biological_processglucose import
A0055056molecular_functionD-glucose transmembrane transporter activity
A0055085biological_processtransmembrane transport
A0065003biological_processprotein-containing complex assembly
A0070062cellular_componentextracellular exosome
A0070837biological_processdehydroascorbic acid transport
A0071260biological_processcellular response to mechanical stimulus
A0071474biological_processcellular hyperosmotic response
A0072562cellular_componentblood microparticle
A0098708biological_processglucose import across plasma membrane
A0098793cellular_componentpresynapse
A0150104biological_processtransport across blood-brain barrier
A1904016biological_processresponse to Thyroglobulin triiodothyronine
A1904659biological_processglucose transmembrane transport
A1990350cellular_componentglucose transporter complex
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue 5RF A 501
ChainResidue
ASER80
ATHR137
AGLN282
APHE379
ATRP388
AGLY408
AASN411
ATRP412

Functional Information from PROSITE/UniProt
site_idPS00216
Number of Residues17
DetailsSUGAR_TRANSPORT_1 Sugar transport proteins signature 1. SLFVVERAGRRtlhli.G
ChainResidueDetails
ASER324-GLY340

site_idPS00217
Number of Residues26
DetailsSUGAR_TRANSPORT_2 Sugar transport proteins signature 2. IiGVYcGLttgfvpmYvgEvsptalR
ChainResidueDetails
AILE128-ARG153

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues144
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24847886
ChainResidueDetails
AMET1-ARG11
AASN88-PHE90
AGLY145-ALA155
ACYS207-PRO271
AGLU329-ARG334
APHE389-PRO401
ALYS451-VAL492

site_idSWS_FT_FI2
Number of Residues21
DetailsTRANSMEM: Helical; Name=1
ChainResidueDetails
ALEU12-ILE33

site_idSWS_FT_FI3
Number of Residues74
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:24847886
ChainResidueDetails
AASN34-SER66
ASER113-GLU120
AASP177-LEU185
ASER294-PRO306
AALA356-SER365
AGLN423-CYS429

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=2
ChainResidueDetails
ALEU67-VAL87

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3
ChainResidueDetails
AGLY91-PHE112

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=4
ChainResidueDetails
AMET121-VAL144

site_idSWS_FT_FI7
Number of Residues20
DetailsTRANSMEM: Helical; Name=5
ChainResidueDetails
ALEU156-LEU176

site_idSWS_FT_FI8
Number of Residues20
DetailsTRANSMEM: Helical; Name=6
ChainResidueDetails
ATRP186-PHE206

site_idSWS_FT_FI9
Number of Residues21
DetailsTRANSMEM: Helical; Name=7
ChainResidueDetails
AILE272-TYR293

site_idSWS_FT_FI10
Number of Residues21
DetailsTRANSMEM: Helical; Name=8
ChainResidueDetails
AVAL307-VAL328

site_idSWS_FT_FI11
Number of Residues20
DetailsTRANSMEM: Helical; Name=9
ChainResidueDetails
ATHR335-LEU355

site_idSWS_FT_FI12
Number of Residues22
DetailsTRANSMEM: Helical; Name=10
ChainResidueDetails
ATYR366-TRP388

site_idSWS_FT_FI13
Number of Residues20
DetailsTRANSMEM: Helical; Name=11
ChainResidueDetails
AALA402-PHE422

site_idSWS_FT_FI14
Number of Residues20
DetailsTRANSMEM: Helical; Name=12
ChainResidueDetails
AGLY430-PHE450

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27078104, ECO:0007744|PDB:5EQI
ChainResidueDetails
ATHR137
AGLN282
ATRP388

site_idSWS_FT_FI16
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:24847886, ECO:0007744|PDB:4PYP
ChainResidueDetails
AASN288
AASN317
AGLU380

site_idSWS_FT_FI17
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:27078104
ChainResidueDetails
AASN411

site_idSWS_FT_FI18
Number of Residues1
DetailsSITE: Not glycosylated => ECO:0000269|PubMed:3839598
ChainResidueDetails
AASN411

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC/PRKCB => ECO:0000269|PubMed:25982116
ChainResidueDetails
ASER226

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER465

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR478

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER490

site_idSWS_FT_FI24
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:3839598
ChainResidueDetails
AASN45

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon