2NS1
Crystal structure of the e. coli ammonia channel AMTB complexed with the signal transduction protein GLNK
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 |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006808 | biological_process | regulation of nitrogen utilization |
B | 0030234 | molecular_function | enzyme regulator activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0045848 | biological_process | positive regulation of nitrogen utilization |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NUU |
Chain | Residue | Details |
B | THR29 | |
A | GLY69-GLN97 | |
A | GLY150-GLY163 | |
A | ALA220-ILE226 | |
A | ILE279-GLY280 | |
A | ALA334-MET348 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9733647, ECO:0007744|PDB:2GNK |
Chain | Residue | Details |
B | GLY37 | |
A | CYS312-ALA333 | |
A | GLY349-ALA377 | |
B | ALA64 | |
B | GLY87 | |
B | ARG101 | |
A | GLY164-ALA179 | |
A | MET200-SER219 | |
A | ALA227-ALA251 | |
A | LEU258-TYR278 | |
A | VAL281-VAL299 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17190799, ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NS1, ECO:0007744|PDB:2NUU |
Chain | Residue | Details |
B | ARG38 | |
A | GLU121-ARG124 | |
A | TYR180-PRO199 | |
A | LEU252-SER257 | |
A | THR300-PRO311 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 |
Chain | Residue | Details |
B | PHE51 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15361618 |
Chain | Residue | Details |
A | SER219 |
site_id | SWS_FT_FI6 |
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_FI7 |
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_FI8 |
Number of Residues | 1 |
Details | SITE: Important for optimum substrate conductance => ECO:0000305|PubMed:18362341 |
Chain | Residue | Details |
A | PHE215 |