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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PZ9

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

Functional Information from GO Data
ChainGOidnamespacecontents
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
C0055085biological_processtransmembrane transport
C0071805biological_processpotassium ion transmembrane transport
C0140359molecular_functionABC-type transporter activity
D0001669cellular_componentacrosomal vesicle
D0002931biological_processresponse to ischemia
D0005242molecular_functioninward rectifier potassium channel activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005635cellular_componentnuclear envelope
D0005737cellular_componentcytoplasm
D0005768cellular_componentendosome
D0005886cellular_componentplasma membrane
D0006813biological_processpotassium ion transport
D0008282cellular_componentinward rectifying potassium channel
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
D0032355biological_processresponse to estradiol
D0033198biological_processresponse to ATP
D0033574biological_processresponse to testosterone
D0042383cellular_componentsarcolemma
D0042734cellular_componentpresynaptic membrane
D0043025cellular_componentneuronal cell body
D0044325molecular_functiontransmembrane transporter binding
D0046676biological_processnegative regulation of insulin secretion
D0055085biological_processtransmembrane transport
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
D1903078biological_processpositive regulation of protein localization to plasma membrane
D1990573biological_processpotassium ion import across plasma membrane
D2001259biological_processpositive regulation of cation channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ATP C 1602
ChainResidue
CTHR404
CSER720
CSER721
CGLN775
CSER405
CASN406
CTRP688
CVAL715
CGLY716
CCYS717
CGLY718
CLYS719
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 Residues15
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues263
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues24
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=13","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=14","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=15","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=16","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=17","evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q09428","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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