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5NKQ

Crystal structure of a dual topology fluoride ion channel.

Replaces:  5FXBReplaces:  5A41
Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0046872molecular_functionmetal ion binding
A0062054molecular_functionfluoride channel activity
A0140114biological_processcellular detoxification of fluoride
A1903424biological_processfluoride transmembrane transport
A1903425molecular_functionfluoride transmembrane transporter activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0046872molecular_functionmetal ion binding
B0062054molecular_functionfluoride channel activity
B0140114biological_processcellular detoxification of fluoride
B1903424biological_processfluoride transmembrane transport
B1903425molecular_functionfluoride transmembrane transporter activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0046872molecular_functionmetal ion binding
C0062054molecular_functionfluoride channel activity
C0140114biological_processcellular detoxification of fluoride
C1903424biological_processfluoride transmembrane transport
C1903425molecular_functionfluoride transmembrane transporter activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0046872molecular_functionmetal ion binding
D0062054molecular_functionfluoride channel activity
D0140114biological_processcellular detoxification of fluoride
D1903424biological_processfluoride transmembrane transport
D1903425molecular_functionfluoride transmembrane transporter activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue NA A 201
ChainResidue
AGLY77
ATHR80
BGLY77
BTHR80

site_idAC2
Number of Residues4
Detailsbinding site for residue F A 202
ChainResidue
AASN43
APHE85
ATYR104
ASER108

site_idAC3
Number of Residues5
Detailsbinding site for residue F A 203
ChainResidue
ASER83
BASN43
BGLY47
BSER112
APHE82

site_idAC4
Number of Residues4
Detailsbinding site for residue F B 201
ChainResidue
BLEU40
BASN43
BTYR104
BSER108

site_idAC5
Number of Residues6
Detailsbinding site for residue F B 202
ChainResidue
AASN43
AGLY47
ATHR80
ASER112
BPHE82
BSER83

site_idAC6
Number of Residues4
Detailsbinding site for residue NA C 201
ChainResidue
CGLY77
CTHR80
DGLY77
DTHR80

site_idAC7
Number of Residues5
Detailsbinding site for residue F C 202
ChainResidue
CASN43
CGLY47
CSER112
DPHE82
DSER83

site_idAC8
Number of Residues5
Detailsbinding site for residue F C 203
ChainResidue
CPHE82
CSER83
DASN43
DGLY47
DSER112

site_idAC9
Number of Residues4
Detailsbinding site for residue F C 204
ChainResidue
CLEU40
CASN43
CTYR104
CSER108

site_idAD1
Number of Residues4
Detailsbinding site for residue F D 201
ChainResidue
DLEU40
DASN43
DTYR104
DSER108

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
EGLY38-PRO45

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues400
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5A40, ECO:0007744|PDB:5NKQ
ChainResidueDetails
ALEU7-LYS29
DALA65-CYS94
APRO36-ILE57
AALA65-CYS94
ATYR98-LEU126
BLEU7-LYS29
BPRO36-ILE57
BALA65-CYS94
BTYR98-LEU126
CLEU7-LYS29
CPRO36-ILE57
CALA65-CYS94
CTYR98-LEU126
DLEU7-LYS29
DPRO36-ILE57
DTYR98-LEU126

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5NKQ
ChainResidueDetails
AASN43
ATYR104
ASER108
ASER112
BASN43
BTYR104
BSER108
BSER112
CASN43
CTYR104
CSER108
CSER112
DASN43
DTYR104
DSER108
DSER112

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00454, ECO:0000269|PubMed:26344196, ECO:0007744|PDB:5NKQ
ChainResidueDetails
AGLY77
ATHR80
BGLY77
BTHR80
CGLY77
CTHR80
DGLY77
DTHR80

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PDB entries from 2024-04-17

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