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4XDL

Crystal structure of human two pore domain potassium ion channel TREK2 (K2P10.1) in complex with a brominated fluoxetine derivative.

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
BILE173
BGLY174
BVAL282
BGLY283
BK401

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 602
ChainResidue
ATHR172
ATHR281
BTHR172
BTHR281
BK401

site_idAC3
Number of Residues3
Detailsbinding site for residue CD A 604
ChainResidue
AGLU113
AGLU116
DASP120

site_idAC4
Number of Residues4
Detailsbinding site for residue 40D A 605
ChainResidue
AVAL253
ALEU279
ATHR280
APHE316

site_idAC5
Number of Residues10
Detailsbinding site for residue K B 401
ChainResidue
ATHR172
AILE173
ATHR281
AVAL282
AK601
AK602
BTHR172
BILE173
BTHR281
BVAL282

site_idAC6
Number of Residues2
Detailsbinding site for residue 40D B 402
ChainResidue
BVAL253
BPHE316

site_idAC7
Number of Residues9
Detailsbinding site for residue K C 601
ChainResidue
CILE173
CGLY174
CVAL282
CGLY283
CK602
DILE173
DGLY174
DVAL282
DGLY283

site_idAC8
Number of Residues10
Detailsbinding site for residue K C 602
ChainResidue
CTHR172
CILE173
CTHR281
CVAL282
CK601
CK603
DTHR172
DILE173
DTHR281
DVAL282

site_idAC9
Number of Residues5
Detailsbinding site for residue K C 603
ChainResidue
CTHR172
CTHR281
CK602
DTHR172
DTHR281

site_idAD1
Number of Residues3
Detailsbinding site for residue 40D C 604
ChainResidue
CVAL253
CTHR280
CPHE316

site_idAD2
Number of Residues3
Detailsbinding site for residue CD D 401
ChainResidue
AASP120
DGLU113
DGLU116

site_idAD3
Number of Residues3
Detailsbinding site for residue 40D D 404
ChainResidue
DVAL253
DTHR280
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:0000255
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:0000255
ChainResidueDetails
AILE263-GLY294
BILE263-GLY294
CILE263-GLY294
DILE263-GLY294

site_idSWS_FT_FI5
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AVAL144
DVAL144
DILE147
DGLY148
AILE147
AGLY148
BVAL144
BILE147
BGLY148
CVAL144
CILE147
CGLY148

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PDB entries from 2024-07-24

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