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

6BX4

The crystal structure of fluoride channel Fluc Ec2 with Monobody S9

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
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
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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue F A 201
ChainResidue
AASN41
AGLY45
ASER110
BPHE80
BSER81
BSER84

site_idAC2
Number of Residues3
Detailsbinding site for residue F A 202
ChainResidue
APHE83
AGLU86
AHOH318

site_idAC3
Number of Residues8
Detailsbinding site for residue DMU A 203
ChainResidue
APHE88
ALEU91
AGLN92
AGLY94
ATYR96
AHOH313
BLEU111
BPHE119

site_idAC4
Number of Residues4
Detailsbinding site for residue NA A 204
ChainResidue
AGLY75
ASER78
BGLY75
BSER78

site_idAC5
Number of Residues5
Detailsbinding site for residue F B 201
ChainResidue
APHE80
ASER81
BASN41
BGLY45
BSER110

site_idAC6
Number of Residues3
Detailsbinding site for residue F B 202
ChainResidue
BPHE83
BGLU86
BVAL87

site_idAC7
Number of Residues12
Detailsbinding site for residue DMU B 203
ChainResidue
AILE108
ALEU111
AILE112
APHE119
BLEU91
BGLN92
BGLY94
BTYR96
BHOH301
BHOH306
BHOH314
DPRO52

Functional Information from PROSITE/UniProt
site_idPS00687
Number of Residues8
DetailsALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. GETGGNSP
ChainResidueDetails
CGLY38-PRO45

225681

PDB entries from 2024-10-02

PDB statisticsPDBj update infoContact PDBjnumon