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7P06

Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in outward-facing conformation with ADP-orthovanadate/ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005886cellular_componentplasma membrane
A0008559molecular_functionABC-type xenobiotic transporter activity
A0009410biological_processresponse to xenobiotic stimulus
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0030003biological_processintracellular monoatomic cation homeostasis
A0042626molecular_functionATPase-coupled transmembrane transporter activity
A0042802molecular_functionidentical protein binding
A0046677biological_processresponse to antibiotic
A0046898biological_processresponse to cycloheximide
A0055085biological_processtransmembrane transport
A0071944cellular_componentcell periphery
A0140359molecular_functionABC-type transporter activity
A1990961biological_processxenobiotic detoxification by transmembrane export across the plasma membrane
Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. VSGGERKRVSIAEVS
ChainResidueDetails
AVAL309-SER323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1033
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-ARG517
AGLU580-LYS611
AHIS651-GLU665
AGLU794-GLN1237
AALA1314-GLY1324
APRO1380-ARG1388
AARG1500-LYS1511

site_idSWS_FT_FI2
Number of Residues246
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AASN518-PHE542
AALA1355-MET1379
AVAL1389-VAL1407
AASN1477-ALA1499
AALA559-TYR579
ALEU612-PHE628
AGLY632-SER650
AALA666-ILE685
APHE775-CYS793
AMET1238-VAL1260
ATRP1292-ASN1313
AALA1325-ASN1349

site_idSWS_FT_FI3
Number of Residues207
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
ALYS543-SER558
AARG629-ASN631
APRO686-GLY774
AGLN1261-PRO1291
AGLN1350-SER1354
AASP1408-ARG1476

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434
ChainResidueDetails
AGLY905

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER22
ASER58

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950
ChainResidueDetails
ATHR49

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR51

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER54
ASER854

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950
ChainResidueDetails
ASER61

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER837

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ASER840
ASER841

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER849
ASER850

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN734
AASN1447

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:12872131, ECO:0000269|PubMed:14557538
ChainResidueDetails
ALYS825

222036

PDB entries from 2024-07-03

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