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6UKN

Cryo-EM structure of the potassium-chloride cotransporter KCC4 in lipid nanodiscs

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0006884biological_processcell volume homeostasis
A0007268biological_processchemical synaptic transmission
A0008519molecular_functionammonium transmembrane transporter activity
A0015293molecular_functionsymporter activity
A0015377molecular_functionchloride:monoatomic cation symporter activity
A0015379molecular_functionpotassium:chloride symporter activity
A0016020cellular_componentmembrane
A0019901molecular_functionprotein kinase binding
A0022857molecular_functiontransmembrane transporter activity
A0032991cellular_componentprotein-containing complex
A0045202cellular_componentsynapse
A0046873molecular_functionmetal ion transmembrane transporter activity
A0055064biological_processchloride ion homeostasis
A0055075biological_processpotassium ion homeostasis
A0055085biological_processtransmembrane transport
A0071333biological_processcellular response to glucose stimulus
A0071805biological_processpotassium ion transmembrane transport
A0098662biological_processinorganic cation transmembrane transport
A0140157biological_processammonium import across plasma membrane
A1902476biological_processchloride transmembrane transport
A1990573biological_processpotassium ion import across plasma membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues455
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
AMET1-MET118
ATHR162-ALA200
AASN274-LYS275
AGLY437-ILE456
ATHR515-GLU553
AGLN599-SER624
AARG866-SER1083

site_idSWS_FT_FI2
Number of Residues240
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AGLY119-LEU139
ALEU141-CYS161
AVAL201-ILE221
AVAL253-VAL273
ALEU276-ILE296
AILE416-ALA436
ALEU457-ILE477
ALEU494-SER514
APRO554-LEU574
AALA578-VAL598
ALEU625-ALA645
AASN845-LEU865

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19144319
ChainResidueDetails
ASER30
ASER33

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19144319
ChainResidueDetails
ATHR37

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER50

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Y666
ChainResidueDetails
ASER62

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR973
ATHR980

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:23376777
ChainResidueDetails
AASN312
AASN360

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19656770, ECO:0000269|PubMed:23376777
ChainResidueDetails
AASN331

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:23376777
ChainResidueDetails
AASN344

219869

PDB entries from 2024-05-15

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