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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7S5V

Human KATP channel in open conformation, focused on SUR

Functional Information from GO Data
ChainGOidnamespacecontents
E0000166molecular_functionnucleotide binding
E0001678biological_processintracellular glucose homeostasis
E0005267molecular_functionpotassium channel activity
E0005524molecular_functionATP binding
E0005886cellular_componentplasma membrane
E0006813biological_processpotassium ion transport
E0007565biological_processfemale pregnancy
E0007613biological_processmemory
E0008281molecular_functionsulfonylurea receptor activity
E0008282cellular_componentinward rectifying potassium channel
E0008542biological_processvisual learning
E0009268biological_processresponse to pH
E0009410biological_processresponse to xenobiotic stimulus
E0010043biological_processresponse to zinc ion
E0010989biological_processnegative regulation of low-density lipoprotein particle clearance
E0015272molecular_functionATP-activated inward rectifier potassium channel activity
E0016020cellular_componentmembrane
E0016525biological_processnegative regulation of angiogenesis
E0016887molecular_functionATP hydrolysis activity
E0019829molecular_functionATPase-coupled monoatomic cation transmembrane transporter activity
E0030672cellular_componentsynaptic vesicle membrane
E0031004cellular_componentpotassium ion-transporting ATPase complex
E0032496biological_processresponse to lipopolysaccharide
E0032760biological_processpositive regulation of tumor necrosis factor production
E0032868biological_processresponse to insulin
E0032991cellular_componentprotein-containing complex
E0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
E0042383cellular_componentsarcolemma
E0042734cellular_componentpresynaptic membrane
E0043268biological_processpositive regulation of potassium ion transport
E0043531molecular_functionADP binding
E0044325molecular_functiontransmembrane transporter binding
E0046676biological_processnegative regulation of insulin secretion
E0046872molecular_functionmetal ion binding
E0050768biological_processnegative regulation of neurogenesis
E0050796biological_processregulation of insulin secretion
E0055085biological_processtransmembrane transport
E0060253biological_processnegative regulation of glial cell proliferation
E0061855biological_processnegative regulation of neuroblast migration
E0071805biological_processpotassium ion transmembrane transport
E0140359molecular_functionABC-type transporter activity
E1900721biological_processpositive regulation of uterine smooth muscle relaxation
E1905075biological_processpositive regulation of tight junction disassembly
E1905604biological_processnegative regulation of blood-brain barrier permeability
E1990573biological_processpotassium ion import across plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRISVARAL
ChainResidueDetails
ELEU830-LEU844
EPHE1482-PHE1496
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues55
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues559
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues17
DetailsTransmembrane: {"description":"Helical; Name=14","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=15","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=16","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues15
DetailsTransmembrane: {"description":"Helical; Name=17","evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues234
DetailsDomain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"29286281","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6C3O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6C3P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q09427","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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