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6PZI

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

Functional Information from GO Data
ChainGOidnamespacecontents
G0000166molecular_functionnucleotide binding
G0005267molecular_functionpotassium channel activity
G0005524molecular_functionATP binding
G0005886cellular_componentplasma membrane
G0006813biological_processpotassium ion transport
G0008281molecular_functionsulfonylurea receptor activity
G0009410biological_processresponse to xenobiotic stimulus
G0016020cellular_componentmembrane
G0016887molecular_functionATP hydrolysis activity
G0022857molecular_functiontransmembrane transporter activity
G0032991cellular_componentprotein-containing complex
G0033198biological_processresponse to ATP
G0042383cellular_componentsarcolemma
G0042626molecular_functionATPase-coupled transmembrane transporter activity
G0046872molecular_functionmetal ion binding
G0055085biological_processtransmembrane transport
G0071805biological_processpotassium ion transmembrane transport
G0140359molecular_functionABC-type transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue ATP G 1601
ChainResidue
GSER405
GTRP688
GGLY716
GCYS717
GGLY718
GLYS719
GSER720
GGLN775

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRISVARAL
ChainResidueDetails
GLEU830-LEU844
GPHE1482-PHE1496

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues110
DetailsTOPO_DOM: Extracellular => ECO:0000305|PubMed:10506167
ChainResidueDetails
GMET1-ALA30
GALA90-LEU106
GPHE154-PHE169
GTYR1032-VAL1067
GTHR1266-VAL1281

site_idSWS_FT_FI2
Number of Residues16
DetailsTRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GLEU31-LEU47

site_idSWS_FT_FI3
Number of Residues856
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:10506167
ChainResidueDetails
GPHE48-ASN72
GTYR124-LEU136
GVAL187-SER303
GLEU593-LEU1013
GMET1298-LYS1582

site_idSWS_FT_FI4
Number of Residues16
DetailsTRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GLEU73-ILE89

site_idSWS_FT_FI5
Number of Residues16
DetailsTRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GTYR107-TYR123

site_idSWS_FT_FI6
Number of Residues16
DetailsTRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GILE137-LYS153

site_idSWS_FT_FI7
Number of Residues16
DetailsTRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GCYS170-GLU186

site_idSWS_FT_FI8
Number of Residues15
DetailsTRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GTHR304-CYS319

site_idSWS_FT_FI9
Number of Residues60
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
GILE320-TYR356
GILE455-ALA460
GTHR558-ALA576
GPRO1162

site_idSWS_FT_FI10
Number of Residues15
DetailsTRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GVAL357-PHE372

site_idSWS_FT_FI11
Number of Residues263
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
GLEU373-LEU438
GGLN474-SER541
GTHR1085-LEU1143
GTYR1176-GLU1249

site_idSWS_FT_FI12
Number of Residues15
DetailsTRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GTRP439-TYR454

site_idSWS_FT_FI13
Number of Residues12
DetailsTRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GLEU461-VAL473

site_idSWS_FT_FI14
Number of Residues15
DetailsTRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GILE542-ILE557

site_idSWS_FT_FI15
Number of Residues15
DetailsTRANSMEM: Helical; Name=11 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GPHE577-LEU592

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=12 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GSER1014-ASP1031

site_idSWS_FT_FI17
Number of Residues16
DetailsTRANSMEM: Helical; Name=13 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GPHE1068-VAL1084

site_idSWS_FT_FI18
Number of Residues17
DetailsTRANSMEM: Helical; Name=14 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GSER1144-THR1161

site_idSWS_FT_FI19
Number of Residues12
DetailsTRANSMEM: Helical; Name=15 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GVAL1163-CYS1175

site_idSWS_FT_FI20
Number of Residues15
DetailsTRANSMEM: Helical; Name=16 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GVAL1250-ALA1265

site_idSWS_FT_FI21
Number of Residues15
DetailsTRANSMEM: Helical; Name=17 => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GGLY1282-TRP1297

site_idSWS_FT_FI22
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q09428
ChainResidueDetails
GTRP688
GSER1386
GSER1387
GSER1483
GGLY716
GSER720
GSER721
GGLN775
GTHR1381
GGLY1382
GGLY1384
GLYS1385

site_idSWS_FT_FI23
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10506167, ECO:0000269|PubMed:8942641
ChainResidueDetails
GASN10

site_idSWS_FT_FI24
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10506167
ChainResidueDetails
GASN1050

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PDB entries from 2025-07-02

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