Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6A70

Structure of the human PKD1/PKD2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0016020cellular_componentmembrane
B0016020cellular_componentmembrane
F0005509molecular_functioncalcium ion binding
F0016020cellular_componentmembrane
G0005509molecular_functioncalcium ion binding
G0016020cellular_componentmembrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AVAL220-MET241
BGLY4028-VAL4048
BTRP4091-TYR4110
FVAL220-MET241
GVAL220-MET241
BGLY3560-PHE3580
BGLY3583-TRP3603
BARG3666-LEU3686
BLEU3902-TRP3922
BTRP3936-LEU3956
BSER3985-GLN4005

site_idSWS_FT_FI2
Number of Residues807
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AMET242-THR468
GTYR527-ALA552
GGLY620-GLU631
GALA647-ARG654
ATYR527-ALA552
AGLY620-GLU631
AALA647-ARG654
FMET242-THR468
FTYR527-ALA552
FGLY620-GLU631
FALA647-ARG654
GMET242-THR468

site_idSWS_FT_FI3
Number of Residues60
DetailsTRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
APHE469-VAL489
FPHE469-VAL489
GPHE469-VAL489
BGLY3957-SER3984
BSER4049-LEU4090

site_idSWS_FT_FI4
Number of Residues114
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AGLU490-SER505
APHE574-LEU597
FGLU490-SER505
FPHE574-LEU597
GGLU490-SER505
GPHE574-LEU597

site_idSWS_FT_FI5
Number of Residues60
DetailsTRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
APHE506-ILE526
FPHE506-ILE526
GPHE506-ILE526

site_idSWS_FT_FI6
Number of Residues60
DetailsTRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
ATYR553-LEU573
FTYR553-LEU573
GTYR553-LEU573

site_idSWS_FT_FI7
Number of Residues63
DetailsTRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
APHE598-PHE619
FPHE598-PHE619
GPHE598-PHE619

site_idSWS_FT_FI8
Number of Residues42
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
ACYS632-PHE646
FCYS632-PHE646
GCYS632-PHE646

site_idSWS_FT_FI9
Number of Residues60
DetailsTRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AVAL655-MET675
FVAL655-MET675
GVAL655-MET675

site_idSWS_FT_FI10
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28092368
ChainResidueDetails
AASN299
AASN305
FASN299
FASN305
GASN299
GASN305

site_idSWS_FT_FI11
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AASN328
FASN328
GASN328

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:27768895, ECO:0000269|PubMed:27991905, ECO:0000269|PubMed:28092368
ChainResidueDetails
AASN362
AASN375
FASN362
FASN375
GASN362
GASN375

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon