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

4XDK

Crystal structure of human two pore domain potassium ion channel TREK2 (K2P10.1) in complex with norfluoxetine

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0016020cellular_componentmembrane
A0071805biological_processpotassium ion transmembrane transport
B0005267molecular_functionpotassium channel activity
B0016020cellular_componentmembrane
B0071805biological_processpotassium ion transmembrane transport
C0005267molecular_functionpotassium channel activity
C0016020cellular_componentmembrane
C0071805biological_processpotassium ion transmembrane transport
D0005267molecular_functionpotassium channel activity
D0016020cellular_componentmembrane
D0071805biological_processpotassium ion transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue K A 601
ChainResidue
AILE173
AGLY174
AVAL282
AGLY283
AK602
BILE173
BGLY174
BVAL282
BGLY283

site_idAC2
Number of Residues10
Detailsbinding site for residue K A 602
ChainResidue
ATHR172
AILE173
ATHR281
AVAL282
AK601
AK603
BTHR172
BILE173
BTHR281
BVAL282

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 603
ChainResidue
ATHR172
ATHR281
AK602
BTHR172
BTHR281

site_idAC4
Number of Residues2
Detailsbinding site for residue PC1 A 604
ChainResidue
AVAL251
ALEU304

site_idAC5
Number of Residues1
Detailsbinding site for residue PC1 A 605
ChainResidue
AARG237

site_idAC6
Number of Residues7
Detailsbinding site for residue 408 A 606
ChainResidue
ACYS249
AVAL253
ALEU279
ATHR280
APHE316
BILE194
BPRO198

site_idAC7
Number of Residues6
Detailsbinding site for residue 405 A 607
ChainResidue
AVAL253
ALEU279
ATHR280
APHE316
BILE194
BPRO198

site_idAC8
Number of Residues9
Detailsbinding site for residue 405 A 608
ChainResidue
AILE194
APRO198
BCYS249
BVAL253
BVAL276
BLEU279
BTHR280
BPHE316
BLEU320

site_idAC9
Number of Residues2
Detailsbinding site for residue PC1 B 401
ChainResidue
BVAL251
BLEU304

site_idAD1
Number of Residues8
Detailsbinding site for residue 408 B 403
ChainResidue
AILE194
APRO198
BCYS249
BVAL253
BVAL276
BLEU279
BTHR280
BPHE316

site_idAD2
Number of Residues9
Detailsbinding site for residue K C 601
ChainResidue
CILE173
CGLY174
CVAL282
CGLY283
CK602
DILE173
DGLY174
DVAL282
DGLY283

site_idAD3
Number of Residues10
Detailsbinding site for residue K C 602
ChainResidue
CTHR172
CILE173
CTHR281
CVAL282
CK601
CK603
DTHR172
DILE173
DTHR281
DVAL282

site_idAD4
Number of Residues5
Detailsbinding site for residue K C 603
ChainResidue
CTHR172
CTHR281
CK602
DTHR172
DTHR281

site_idAD5
Number of Residues9
Detailsbinding site for residue 408 C 604
ChainResidue
CCYS249
CVAL253
CVAL276
CLEU279
CTHR280
CPHE316
DILE194
DILE197
DPRO198

site_idAD6
Number of Residues8
Detailsbinding site for residue 405 C 605
ChainResidue
DPRO198
CCYS249
CVAL253
CVAL276
CLEU279
CTHR280
CPHE316
DILE194

site_idAD7
Number of Residues8
Detailsbinding site for residue 408 C 606
ChainResidue
CILE194
CILE197
CPRO198
DVAL253
DLEU279
DTHR280
DLEU313
DPHE316

site_idAD8
Number of Residues6
Detailsbinding site for residue 405 C 607
ChainResidue
CILE194
CPRO198
DVAL253
DLEU279
DLEU313
DPHE316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues320
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
AMET72-GLY92
CTHR182-PHE202
CTHR234-THR254
CGLU299-VAL319
DMET72-GLY92
DTHR182-PHE202
DTHR234-THR254
DGLU299-VAL319
ATHR182-PHE202
ATHR234-THR254
AGLU299-VAL319
BMET72-GLY92
BTHR182-PHE202
BTHR234-THR254
BGLU299-VAL319
CMET72-GLY92

site_idSWS_FT_FI2
Number of Residues104
DetailsINTRAMEM: Pore-forming; Name=Pore-forming 1 => ECO:0007744|PDB:4BW5
ChainResidueDetails
ASER154-PRO180
BSER154-PRO180
CSER154-PRO180
DSER154-PRO180

site_idSWS_FT_FI3
Number of Residues120
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ALEU203-GLN233
BLEU203-GLN233
CLEU203-GLN233
DLEU203-GLN233

site_idSWS_FT_FI4
Number of Residues124
DetailsINTRAMEM: Pore-forming; Name=Pore-forming 2 => ECO:0007744|PDB:4BW5
ChainResidueDetails
AILE263-GLY294
BILE263-GLY294
CILE263-GLY294
DILE263-GLY294

site_idSWS_FT_FI5
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:25766236, ECO:0007744|PDB:4XDK
ChainResidueDetails
AGLY167
BTHR168
BVAL169
BILE170
BVAL276
BVAL277
BTHR278
BLEU279
CGLY167
CTHR168
CVAL169
ATHR168
CILE170
CVAL276
CVAL277
CTHR278
CLEU279
DGLY167
DTHR168
DVAL169
DILE170
DVAL276
AVAL169
DVAL277
DTHR278
DLEU279
AILE170
AVAL276
AVAL277
ATHR278
ALEU279
BGLY167

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: pH sensor => ECO:0000250|UniProtKB:Q8BUW1
ChainResidueDetails
ASER151
BSER151
CSER151
DSER151

site_idSWS_FT_FI7
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AVAL144
DVAL144
DILE147
DGLY148
AILE147
AGLY148
BVAL144
BILE147
BGLY148
CVAL144
CILE147
CGLY148

225946

PDB entries from 2024-10-09

PDB statisticsPDBj update infoContact PDBjnumon