Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WLK

STRUCTURE OF THE ATP-SENSITIVE INWARD RECTIFIER POTASSIUM CHANNEL FROM MAGNETOSPIRILLUM MAGNETOTACTICUM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005242molecular_functioninward rectifier potassium channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0034765biological_processregulation of monoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A1990573biological_processpotassium ion import across plasma membrane
B0005242molecular_functioninward rectifier potassium channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0034765biological_processregulation of monoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B1990573biological_processpotassium ion import across plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K A 1302
ChainResidue
ATHR96
BTHR96
BILE97
BILE97
ATHR96
AILE97
AILE97
AK1303
AK1303
AK1304
AK1304
BTHR96

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1303
ChainResidue
ATHR96
ATHR96
AK1302
AK1302
BTHR96
BTHR96

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE K A 1304
ChainResidue
AILE97
AILE97
AGLY98
AGLY98
AK1302
AK1302
AK1305
AK1305
BILE97
BILE97
BGLY98
BGLY98

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE K A 1305
ChainResidue
AGLY98
AGLY98
ATYR99
ATYR99
AK1304
AK1304
BGLY98
BGLY98
BTYR99
BTYR99

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SPM B 1302
ChainResidue
ATYR132
ATYR132
BTYR132
BTYR132
BHOH2018
BHOH2018
BHOH2019
BHOH2019

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1306
ChainResidue
AARG194
BARG202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues90
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsIntramembrane: {"description":"Helical; Pore-forming"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues326
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsMotif: {"description":"Selectivity filter"}
ChainResidueDetails

242500

PDB entries from 2025-10-01

PDB statisticsPDBj update infoContact PDBjnumon