1U77
Crystal Structure of Ammonia Channel AmtB from E. Coli
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0008519 | molecular_function | ammonium channel activity |
A | 0015670 | biological_process | carbon dioxide transport |
A | 0016020 | cellular_component | membrane |
A | 0042802 | molecular_function | identical protein binding |
A | 0072488 | biological_process | ammonium transmembrane transport |
Functional Information from PROSITE/UniProt
site_id | PS01219 |
Number of Residues | 26 |
Details | AMMONIUM_TRANSP Ammonium transporters signature. DFAGGtvVhinAAiaGLvgaYLiGkR |
Chain | Residue | Details |
A | ASP160-ARG185 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 71 |
Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 |
Chain | Residue | Details |
A | ALA1-ASN10 | |
A | GLY69-GLN97 | |
A | GLY150-GLY163 | |
A | ALA220-ILE226 | |
A | ILE279-GLY280 | |
A | ALA334-MSE348 |
site_id | SWS_FT_FI2 |
Number of Residues | 236 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 |
Chain | Residue | Details |
A | ALA11-TYR32 | |
A | CYS312-ALA333 | |
A | GLY349-ALA377 | |
A | MSE44-SER68 | |
A | TYR98-ALA120 | |
A | PHE125-GLY149 | |
A | GLY164-ALA179 | |
A | MSE200-SER219 | |
A | ALA227-ALA251 | |
A | LEU258-TYR278 | |
A | VAL281-VAL299 |
site_id | SWS_FT_FI3 |
Number of Residues | 48 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:15361618, ECO:0000269|PubMed:15563598, ECO:0000269|PubMed:17040913 |
Chain | Residue | Details |
A | GLY33-SER43 | |
A | GLU121-ARG124 | |
A | TYR180-PRO199 | |
A | LEU252-SER257 | |
A | THR300-PRO311 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15361618 |
Chain | Residue | Details |
A | SER219 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for the deprotonation of the ammonium cation => ECO:0000269|PubMed:19278252 |
Chain | Residue | Details |
A | ASP160 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | SITE: Twin-His motif. Important for optimum substrate conductance => ECO:0000305|PubMed:17040913, ECO:0000305|PubMed:23667517, ECO:0000305|PubMed:32662768 |
Chain | Residue | Details |
A | HIS168 | |
A | HIS318 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Important for optimum substrate conductance => ECO:0000305|PubMed:18362341 |
Chain | Residue | Details |
A | PHE215 |