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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PZA

Cryo-EM structure of the pancreatic beta-cell SUR1 bound to ATP and glibenclamide

Functional Information from GO Data
ChainGOidnamespacecontents
C0000166molecular_functionnucleotide binding
C0005267molecular_functionpotassium channel activity
C0005524molecular_functionATP binding
C0005886cellular_componentplasma membrane
C0006813biological_processpotassium ion transport
C0008281molecular_functionsulfonylurea receptor activity
C0009410biological_processresponse to xenobiotic stimulus
C0016020cellular_componentmembrane
C0016887molecular_functionATP hydrolysis activity
C0022857molecular_functiontransmembrane transporter activity
C0032991cellular_componentprotein-containing complex
C0033198biological_processresponse to ATP
C0042383cellular_componentsarcolemma
C0042626molecular_functionATPase-coupled transmembrane transporter activity
C0046872molecular_functionmetal ion binding
C0055085biological_processtransmembrane transport
C0071805biological_processpotassium ion transmembrane transport
C0140359molecular_functionABC-type transporter activity
D0000166molecular_functionnucleotide binding
D0001508biological_processaction potential
D0001666biological_processresponse to hypoxia
D0001669cellular_componentacrosomal vesicle
D0002931biological_processresponse to ischemia
D0003229biological_processventricular cardiac muscle tissue development
D0005242molecular_functioninward rectifier potassium channel activity
D0005249molecular_functionvoltage-gated potassium channel activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005635cellular_componentnuclear envelope
D0005737cellular_componentcytoplasm
D0005768cellular_componentendosome
D0005886cellular_componentplasma membrane
D0006006biological_processglucose metabolic process
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0006915biological_processapoptotic process
D0006950biological_processresponse to stress
D0008282cellular_componentinward rectifying potassium channel
D0008340biological_processdetermination of adult lifespan
D0009410biological_processresponse to xenobiotic stimulus
D0014704cellular_componentintercalated disc
D0015272molecular_functionATP-activated inward rectifier potassium channel activity
D0016020cellular_componentmembrane
D0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
D0030315cellular_componentT-tubule
D0030506molecular_functionankyrin binding
D0030673cellular_componentaxolemma
D0031072molecular_functionheat shock protein binding
D0031669biological_processcellular response to nutrient levels
D0032355biological_processresponse to estradiol
D0033198biological_processresponse to ATP
D0033574biological_processresponse to testosterone
D0034220biological_processmonoatomic ion transmembrane transport
D0034702cellular_componentmonoatomic ion channel complex
D0042383cellular_componentsarcolemma
D0042391biological_processregulation of membrane potential
D0042734cellular_componentpresynaptic membrane
D0043025cellular_componentneuronal cell body
D0044325molecular_functiontransmembrane transporter binding
D0046676biological_processnegative regulation of insulin secretion
D0046872molecular_functionmetal ion binding
D0050796biological_processregulation of insulin secretion
D0050877biological_processnervous system process
D0055085biological_processtransmembrane transport
D0061762biological_processCAMKK-AMPK signaling cascade
D0070852cellular_componentcell body fiber
D0071316biological_processcellular response to nicotine
D0071333biological_processcellular response to glucose stimulus
D0071356biological_processcellular response to tumor necrosis factor
D0098978cellular_componentglutamatergic synapse
D0099505biological_processregulation of presynaptic membrane potential
D0099508molecular_functionvoltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential
D1903078biological_processpositive regulation of protein localization to plasma membrane
D1904638biological_processresponse to resveratrol
D1990573biological_processpotassium ion import across plasma membrane
D2001259biological_processpositive regulation of cation channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue GBM C 1601
ChainResidue
CARG306
CTHR1242
CASN1245
CARG1246
CARG1300
DARG4
DLYS5
CTYR377
CILE381
CPHE433
CLEU434
CASN437
CLEU592
CSER1238
CLEU1241
site_idAC2
Number of Residues9
Detailsbinding site for residue ATP C 1602
ChainResidue
CTHR404
CTRP688
CGLY716
CCYS717
CGLY718
CLYS719
CSER720
CSER721
CGLN775
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRISVARAL
ChainResidueDetails
CLEU830-LEU844
CPHE1482-PHE1496
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"10506167","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues152
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"10506167","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues60
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues263
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=13","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=14","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=15","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=16","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=17","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues303
DetailsDomain: {"description":"ABC transmembrane type-1 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"10506167","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8942641","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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