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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6LYY

Cryo-EM structure of the human MCT1/Basigin-2 complex in the presence of anti-cancer drug candidate AZD3965 in the outward-open conformation.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005813cellular_componentcentrosome
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0007098biological_processcentrosome cycle
A0008028molecular_functionmonocarboxylic acid transmembrane transporter activity
A0009925cellular_componentbasal plasma membrane
A0015129molecular_functionlactate transmembrane transporter activity
A0015130molecular_functionmevalonate transmembrane transporter activity
A0015141molecular_functionsuccinate transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015295molecular_functionsolute:proton symporter activity
A0015355molecular_functionsecondary active monocarboxylate transmembrane transporter activity
A0015650molecular_functionlactate:proton symporter activity
A0015718biological_processmonocarboxylic acid transport
A0015728biological_processmevalonate transport
A0016020cellular_componentmembrane
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016328cellular_componentlateral plasma membrane
A0022857molecular_functiontransmembrane transporter activity
A0030054cellular_componentcell junction
A0032094biological_processresponse to food
A0035873biological_processlactate transmembrane transport
A0035879biological_processplasma membrane lactate transport
A0042593biological_processglucose homeostasis
A0042802molecular_functionidentical protein binding
A0042867biological_processpyruvate catabolic process
A0045202cellular_componentsynapse
A0046943molecular_functioncarboxylic acid transmembrane transporter activity
A0050796biological_processregulation of insulin secretion
A0051780biological_processbehavioral response to nutrient
A0055085biological_processtransmembrane transport
A0070062cellular_componentextracellular exosome
A0071422biological_processsuccinate transmembrane transport
A0150104biological_processtransport across blood-brain barrier
A1901475biological_processpyruvate transmembrane transport
A1902600biological_processproton transmembrane transport
A1905039biological_processcarboxylic acid transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue EY0 A 601
ChainResidue
ATYR34
ALEU305
AASP309
AARG313
APHE367
ASER371
ALYS38
ALEU66
ATYR70
AMET151
ASER154
APRO155
ALEU158
ALEU281
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues36
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues39
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7CKO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LZ0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"33333023","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LYY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues94
DetailsDomain: {"description":"Ig-like V-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00114","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsRegion: {"description":"Essential for interaction with KDR/VEGFR2","evidences":[{"source":"PubMed","id":"25825981","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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