8XB3
Structural mechanism of substrate binding and inhibition of the human Norepinephrine Transporter
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0006974 | biological_process | DNA damage response |
A | 0008218 | biological_process | bioluminescence |
A | 0008643 | biological_process | carbohydrate transport |
A | 0015144 | molecular_function | carbohydrate transmembrane transporter activity |
A | 0015768 | biological_process | maltose transport |
A | 0016020 | cellular_component | membrane |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0034219 | biological_process | carbohydrate transmembrane transport |
A | 0034289 | biological_process | detection of maltose stimulus |
A | 0042597 | cellular_component | periplasmic space |
A | 0042956 | biological_process | maltodextrin transmembrane transport |
A | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
A | 0055052 | cellular_component | ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing |
A | 0055085 | biological_process | transmembrane transport |
A | 0060326 | biological_process | cell chemotaxis |
A | 1901982 | molecular_function | maltose binding |
A | 1990060 | cellular_component | maltose transport complex |
Functional Information from PROSITE/UniProt
site_id | PS00610 |
Number of Residues | 15 |
Details | NA_NEUROTRAN_SYMP_1 Sodium:neurotransmitter symporter family signature 1. WRFPYlcykNGGGaF |
Chain | Residue | Details |
A | TRP80-PHE94 |
site_id | PS00754 |
Number of Residues | 21 |
Details | NA_NEUROTRAN_SYMP_2 Sodium:neurotransmitter symporter family signature 2. YLfsSFTlnLPWtdCghtwNS |
Chain | Residue | Details |
A | TYR162-SER182 |
site_id | PS01037 |
Number of Residues | 18 |
Details | SBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN |
Chain | Residue | Details |
A | PRO-218-ASN-201 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | ILE63-LYS88 |
site_id | SWS_FT_FI2 |
Number of Residues | 134 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | ASN89-GLY92 | |
A | PHE167-ILE230 | |
A | THR283-THR306 | |
A | SER363-THR402 | |
A | GLY465 | |
A | ASP546-TYR548 |
site_id | SWS_FT_FI3 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | ALA93-LEU116 |
site_id | SWS_FT_FI4 |
Number of Residues | 115 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | GLY117-LYS135 | |
A | GLY255-LYS257 | |
A | ASN333-ASN338 | |
A | THR429-LYS443 | |
A | SER493-LYS522 | |
A | PRO570-ILE617 |
site_id | SWS_FT_FI5 |
Number of Residues | 30 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | GLY136-SER166 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | GLN234-LYS254 |
site_id | SWS_FT_FI7 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | THR258-VAL282 |
site_id | SWS_FT_FI8 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | VAL307-TYR332 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | CYS339-PHE362 |
site_id | SWS_FT_FI10 |
Number of Residues | 25 |
Details | TRANSMEM: Helical; Name=8 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | PHE403-ILE428 |
site_id | SWS_FT_FI11 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=9 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | LEU444-GLY464 |
site_id | SWS_FT_FI12 |
Number of Residues | 26 |
Details | TRANSMEM: Helical; Name=10 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | ILE466-VAL492 |
site_id | SWS_FT_FI13 |
Number of Residues | 22 |
Details | TRANSMEM: Helical; Name=11 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | PHE523-TYR545 |
site_id | SWS_FT_FI14 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=12 => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | ILE549-VAL569 |
site_id | SWS_FT_FI15 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q7K4Y6 |
Chain | Residue | Details |
A | GLY71 | |
A | ALA73 | |
A | VAL74 | |
A | ASN78 | |
A | SER318 | |
A | ASN350 | |
A | LEU415 | |
A | ASP418 | |
A | SER419 |
site_id | SWS_FT_FI16 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN184 | |
A | GLY190 | |
A | ALA190 |