8OO1
Wide inward-open liganded UraA in complex with a conformation-selective synthetic nanobody
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005886 | cellular_component | plasma membrane |
A | 0015205 | molecular_function | nucleobase transmembrane transporter activity |
A | 0015210 | molecular_function | uracil transmembrane transporter activity |
A | 0015293 | molecular_function | symporter activity |
A | 0015505 | molecular_function | uracil:monoatomic cation symporter activity |
A | 0015857 | biological_process | uracil transport |
A | 0016020 | cellular_component | membrane |
A | 0022857 | molecular_function | transmembrane transporter activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0055085 | biological_process | transmembrane transport |
A | 0098721 | biological_process | uracil import across plasma membrane |
C | 0005886 | cellular_component | plasma membrane |
C | 0015205 | molecular_function | nucleobase transmembrane transporter activity |
C | 0015210 | molecular_function | uracil transmembrane transporter activity |
C | 0015293 | molecular_function | symporter activity |
C | 0015505 | molecular_function | uracil:monoatomic cation symporter activity |
C | 0015857 | biological_process | uracil transport |
C | 0016020 | cellular_component | membrane |
C | 0022857 | molecular_function | transmembrane transporter activity |
C | 0042803 | molecular_function | protein homodimerization activity |
C | 0055085 | biological_process | transmembrane transport |
C | 0098721 | biological_process | uracil import across plasma membrane |
Functional Information from PROSITE/UniProt
site_id | PS01116 |
Number of Residues | 21 |
Details | XANTH_URACIL_PERMASE Xanthine/uracil permeases family signature. IPlPVMGGvsllLYGvIgasG |
Chain | Residue | Details |
A | ILE329-GLY349 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 396 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | LEU14-VAL37 | |
A | VAL333-ILE354 | |
C | LEU14-VAL37 | |
C | ASN42-CYS61 | |
C | ALA90-LYS110 | |
C | ALA123-ALA144 | |
C | SER156-LEU171 | |
C | PHE179-MET199 | |
C | TRP225-VAL248 | |
C | GLY262-GLY281 | |
C | SER302-VAL319 | |
A | ASN42-CYS61 | |
C | VAL333-ILE354 | |
A | ALA90-LYS110 | |
A | ALA123-ALA144 | |
A | SER156-LEU171 | |
A | PHE179-MET199 | |
A | TRP225-VAL248 | |
A | GLY262-GLY281 | |
A | SER302-VAL319 |
site_id | SWS_FT_FI2 |
Number of Residues | 112 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | LEU38-ILE41 | |
C | PRO320-PRO332 | |
A | LEU82-VAL89 | |
A | GLY145-ASP155 | |
A | GLY200-GLU224 | |
A | PRO320-PRO332 | |
C | LEU38-ILE41 | |
C | LEU82-VAL89 | |
C | GLY145-ASP155 | |
C | GLY200-GLU224 |
site_id | SWS_FT_FI3 |
Number of Residues | 140 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | LYS62-LYS64 | |
C | GLY172-GLY178 | |
C | THR249-PRO261 | |
C | ARG299-TYR301 | |
C | GLU355-ASN365 | |
C | LEU402-LYS429 | |
A | ALA111-PRO122 | |
A | GLY172-GLY178 | |
A | THR249-PRO261 | |
A | ARG299-TYR301 | |
A | GLU355-ASN365 | |
A | LEU402-LYS429 | |
C | LYS62-LYS64 | |
C | ALA111-PRO122 |
site_id | SWS_FT_FI4 |
Number of Residues | 64 |
Details | TRANSMEM: Discontinuously helical => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | ILE65-LEU81 | |
A | SER282-THR298 | |
C | ILE65-LEU81 | |
C | SER282-THR298 |
site_id | SWS_FT_FI5 |
Number of Residues | 70 |
Details | INTRAMEM: Discontinuously helical => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | LEU366-GLY401 | |
C | LEU366-GLY401 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21423164 |
Chain | Residue | Details |
A | PHE73 | |
A | GLU241 | |
A | GLY289 | |
A | GLU290 | |
C | PHE73 | |
C | GLU241 | |
C | GLY289 | |
C | GLU290 |