2NUU
Regulating the Escherichia coli ammonia channel: the crystal structure of the AmtB-GlnK complex
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 transmembrane transporter 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 | 0005886 | cellular_component | plasma membrane |
| B | 0008519 | molecular_function | ammonium transmembrane transporter activity |
| B | 0015670 | biological_process | carbon dioxide transport |
| B | 0016020 | cellular_component | membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0072488 | biological_process | ammonium transmembrane transport |
| C | 0005515 | molecular_function | protein binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008519 | molecular_function | ammonium transmembrane transporter activity |
| C | 0015670 | biological_process | carbon dioxide transport |
| C | 0016020 | cellular_component | membrane |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0072488 | biological_process | ammonium transmembrane transport |
| D | 0005515 | molecular_function | protein binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008519 | molecular_function | ammonium transmembrane transporter activity |
| D | 0015670 | biological_process | carbon dioxide transport |
| D | 0016020 | cellular_component | membrane |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0072488 | biological_process | ammonium transmembrane transport |
| E | 0005515 | molecular_function | protein binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0008519 | molecular_function | ammonium transmembrane transporter activity |
| E | 0015670 | biological_process | carbon dioxide transport |
| E | 0016020 | cellular_component | membrane |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0072488 | biological_process | ammonium transmembrane transport |
| F | 0005515 | molecular_function | protein binding |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0008519 | molecular_function | ammonium transmembrane transporter activity |
| F | 0015670 | biological_process | carbon dioxide transport |
| F | 0016020 | cellular_component | membrane |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0072488 | biological_process | ammonium transmembrane transport |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0005886 | cellular_component | plasma membrane |
| G | 0006808 | biological_process | regulation of nitrogen utilization |
| G | 0016020 | cellular_component | membrane |
| G | 0030234 | molecular_function | enzyme regulator activity |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0045848 | biological_process | positive regulation of nitrogen utilization |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0006808 | biological_process | regulation of nitrogen utilization |
| H | 0016020 | cellular_component | membrane |
| H | 0030234 | molecular_function | enzyme regulator activity |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0045848 | biological_process | positive regulation of nitrogen utilization |
| I | 0000166 | molecular_function | nucleotide binding |
| I | 0005515 | molecular_function | protein binding |
| I | 0005524 | molecular_function | ATP binding |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0006808 | biological_process | regulation of nitrogen utilization |
| I | 0016020 | cellular_component | membrane |
| I | 0030234 | molecular_function | enzyme regulator activity |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0045848 | biological_process | positive regulation of nitrogen utilization |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0005515 | molecular_function | protein binding |
| J | 0005524 | molecular_function | ATP binding |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0005829 | cellular_component | cytosol |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0006808 | biological_process | regulation of nitrogen utilization |
| J | 0016020 | cellular_component | membrane |
| J | 0030234 | molecular_function | enzyme regulator activity |
| J | 0042802 | molecular_function | identical protein binding |
| J | 0045848 | biological_process | positive regulation of nitrogen utilization |
| K | 0000166 | molecular_function | nucleotide binding |
| K | 0005515 | molecular_function | protein binding |
| K | 0005524 | molecular_function | ATP binding |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0005829 | cellular_component | cytosol |
| K | 0005886 | cellular_component | plasma membrane |
| K | 0006808 | biological_process | regulation of nitrogen utilization |
| K | 0016020 | cellular_component | membrane |
| K | 0030234 | molecular_function | enzyme regulator activity |
| K | 0042802 | molecular_function | identical protein binding |
| K | 0045848 | biological_process | positive regulation of nitrogen utilization |
| L | 0000166 | molecular_function | nucleotide binding |
| L | 0005515 | molecular_function | protein binding |
| L | 0005524 | molecular_function | ATP binding |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0005829 | cellular_component | cytosol |
| L | 0005886 | cellular_component | plasma membrane |
| L | 0006808 | biological_process | regulation of nitrogen utilization |
| L | 0016020 | cellular_component | membrane |
| L | 0030234 | molecular_function | enzyme regulator activity |
| L | 0042802 | molecular_function | identical protein binding |
| L | 0045848 | biological_process | positive regulation of nitrogen utilization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ADP G 1200 |
| Chain | Residue |
| G | GLY27 |
| H | GLY35 |
| H | PHE36 |
| H | ARG38 |
| H | GLN39 |
| H | LYS58 |
| H | GLY87 |
| H | ASP88 |
| H | GLY89 |
| H | LYS90 |
| H | HOH1308 |
| G | LEU28 |
| G | THR29 |
| G | ASP62 |
| G | VAL63 |
| G | ALA64 |
| G | ARG101 |
| G | ARG103 |
| G | HOH1411 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP H 1300 |
| Chain | Residue |
| H | GLY27 |
| H | LEU28 |
| H | THR29 |
| H | ASP62 |
| H | VAL63 |
| H | ALA64 |
| H | ARG101 |
| H | ARG103 |
| H | HOH1315 |
| I | GLY35 |
| I | PHE36 |
| I | GLY37 |
| I | ARG38 |
| I | GLN39 |
| I | GLY87 |
| I | LYS90 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP G 1400 |
| Chain | Residue |
| G | ILE7 |
| G | GLY35 |
| G | PHE36 |
| G | ARG38 |
| G | GLN39 |
| G | LYS58 |
| G | GLY87 |
| G | ASP88 |
| G | GLY89 |
| G | LYS90 |
| G | HOH1403 |
| G | HOH1407 |
| I | GLY27 |
| I | LEU28 |
| I | THR29 |
| I | ASP62 |
| I | VAL63 |
| I | ALA64 |
| I | ARG101 |
| I | ARG103 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP J 1500 |
| Chain | Residue |
| J | GLY27 |
| J | LEU28 |
| J | THR29 |
| J | ASP62 |
| J | VAL63 |
| J | ALA64 |
| J | ARG101 |
| J | ARG103 |
| J | LEU112 |
| J | HOH1707 |
| K | ILE7 |
| K | GLY35 |
| K | PHE36 |
| K | ARG38 |
| K | GLN39 |
| K | LYS58 |
| K | GLY87 |
| K | ASP88 |
| K | GLY89 |
| K | LYS90 |
| K | HOH121 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ADP L 1600 |
| Chain | Residue |
| K | GLY27 |
| K | LEU28 |
| K | THR29 |
| K | ASP62 |
| K | VAL63 |
| K | ALA64 |
| K | ARG101 |
| K | ARG103 |
| L | ILE7 |
| L | GLY35 |
| L | PHE36 |
| L | GLY37 |
| L | ARG38 |
| L | GLN39 |
| L | LYS58 |
| L | GLY87 |
| L | ASP88 |
| L | GLY89 |
| L | LYS90 |
| L | PHE92 |
| L | HOH1610 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP J 1700 |
| Chain | Residue |
| J | GLY37 |
| J | ARG38 |
| J | GLN39 |
| J | LYS58 |
| J | GLY87 |
| J | ASP88 |
| J | GLY89 |
| J | LYS90 |
| J | HOH1712 |
| J | HOH1714 |
| L | GLY27 |
| L | LEU28 |
| L | THR29 |
| L | ASP62 |
| L | VAL63 |
| L | ALA64 |
| L | ARG101 |
| L | ARG103 |
| J | GLY35 |
| J | PHE36 |
Functional Information from PROSITE/UniProt
| site_id | PS00496 |
| Number of Residues | 6 |
| Details | PII_GLNB_UMP P-II protein uridylation site. YRGAEY |
| Chain | Residue | Details |
| G | TYR46-TYR51 |
| site_id | PS00638 |
| Number of Residues | 14 |
| Details | PII_GLNB_CTER P-II protein C-terminal region signature. TgkiGDGKIFVaeL |
| Chain | Residue | Details |
| G | THR83-LEU96 |
| 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 | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NUU |
| Chain | Residue | Details |
| G | THR29 | |
| A | CYS312-ALA333 | |
| A | GLY349-ALA377 | |
| B | ALA11-TYR32 | |
| B | MET44-PHE68 | |
| B | TYR98-ALA120 | |
| B | PHE125-GLY149 | |
| B | GLY164-ALA179 | |
| B | MET200-SER219 | |
| B | ALA227-ALA251 | |
| B | LEU258-TYR278 | |
| H | THR29 | |
| B | VAL281-VAL299 | |
| B | CYS312-ALA333 | |
| B | GLY349-ALA377 | |
| C | ALA11-TYR32 | |
| C | MET44-PHE68 | |
| C | TYR98-ALA120 | |
| C | PHE125-GLY149 | |
| C | GLY164-ALA179 | |
| C | MET200-SER219 | |
| C | ALA227-ALA251 | |
| I | THR29 | |
| C | LEU258-TYR278 | |
| C | VAL281-VAL299 | |
| C | CYS312-ALA333 | |
| C | GLY349-ALA377 | |
| D | ALA11-TYR32 | |
| D | MET44-PHE68 | |
| D | TYR98-ALA120 | |
| D | PHE125-GLY149 | |
| D | GLY164-ALA179 | |
| D | MET200-SER219 | |
| J | THR29 | |
| D | ALA227-ALA251 | |
| D | LEU258-TYR278 | |
| D | VAL281-VAL299 | |
| D | CYS312-ALA333 | |
| D | GLY349-ALA377 | |
| E | ALA11-TYR32 | |
| E | MET44-PHE68 | |
| E | TYR98-ALA120 | |
| E | PHE125-GLY149 | |
| E | GLY164-ALA179 | |
| K | THR29 | |
| E | MET200-SER219 | |
| E | ALA227-ALA251 | |
| E | LEU258-TYR278 | |
| E | VAL281-VAL299 | |
| E | CYS312-ALA333 | |
| E | GLY349-ALA377 | |
| F | ALA11-TYR32 | |
| F | MET44-PHE68 | |
| F | TYR98-ALA120 | |
| F | PHE125-GLY149 | |
| L | THR29 | |
| F | GLY164-ALA179 | |
| F | MET200-SER219 | |
| F | ALA227-ALA251 | |
| F | LEU258-TYR278 | |
| F | VAL281-VAL299 | |
| F | CYS312-ALA333 | |
| F | GLY349-ALA377 | |
| A | ALA227-ALA251 | |
| A | LEU258-TYR278 | |
| A | VAL281-VAL299 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9733647, ECO:0007744|PDB:2GNK |
| Chain | Residue | Details |
| G | GLY37 | |
| I | ALA64 | |
| I | GLY87 | |
| I | ARG101 | |
| J | GLY37 | |
| J | ALA64 | |
| J | GLY87 | |
| J | ARG101 | |
| K | GLY37 | |
| K | ALA64 | |
| K | GLY87 | |
| G | ALA64 | |
| K | ARG101 | |
| L | GLY37 | |
| L | ALA64 | |
| L | GLY87 | |
| L | ARG101 | |
| E | THR300-PRO311 | |
| F | GLY33-SER43 | |
| F | GLU121-ARG124 | |
| F | TYR180-PRO199 | |
| F | LEU252-SER257 | |
| G | GLY87 | |
| F | THR300-PRO311 | |
| G | ARG101 | |
| H | GLY37 | |
| H | ALA64 | |
| H | GLY87 | |
| H | ARG101 | |
| I | GLY37 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17190799, ECO:0000269|PubMed:17220269, ECO:0007744|PDB:2NS1, ECO:0007744|PDB:2NUU |
| Chain | Residue | Details |
| G | ARG38 | |
| B | ALA334-MET348 | |
| C | GLY69-GLN97 | |
| C | GLY150-GLY163 | |
| C | ALA220-ILE226 | |
| C | ILE279-GLY280 | |
| C | ALA334-MET348 | |
| D | GLY69-GLN97 | |
| D | GLY150-GLY163 | |
| D | ALA220-ILE226 | |
| D | ILE279-GLY280 | |
| H | ARG38 | |
| D | ALA334-MET348 | |
| E | GLY69-GLN97 | |
| E | GLY150-GLY163 | |
| E | ALA220-ILE226 | |
| E | ILE279-GLY280 | |
| E | ALA334-MET348 | |
| F | GLY69-GLN97 | |
| F | GLY150-GLY163 | |
| F | ALA220-ILE226 | |
| F | ILE279-GLY280 | |
| I | ARG38 | |
| F | ALA334-MET348 | |
| J | ARG38 | |
| K | ARG38 | |
| L | ARG38 | |
| B | GLY150-GLY163 | |
| B | ALA220-ILE226 | |
| B | ILE279-GLY280 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: O-UMP-tyrosine => ECO:0000255|PROSITE-ProRule:PRU00675 |
| Chain | Residue | Details |
| G | TYR51 | |
| H | TYR51 | |
| I | TYR51 | |
| J | TYR51 | |
| K | TYR51 | |
| L | TYR51 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15361618 |
| Chain | Residue | Details |
| A | SER219 | |
| B | SER219 | |
| C | SER219 | |
| D | SER219 | |
| E | SER219 | |
| F | SER219 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | SITE: Important for the deprotonation of the ammonium cation => ECO:0000269|PubMed:19278252 |
| Chain | Residue | Details |
| A | ASP160 | |
| B | ASP160 | |
| C | ASP160 | |
| D | ASP160 | |
| E | ASP160 | |
| F | ASP160 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| 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 | |
| E | HIS318 | |
| F | HIS168 | |
| F | HIS318 | |
| A | HIS318 | |
| B | HIS168 | |
| B | HIS318 | |
| C | HIS168 | |
| C | HIS318 | |
| D | HIS168 | |
| D | HIS318 | |
| E | HIS168 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | SITE: Important for optimum substrate conductance => ECO:0000305|PubMed:18362341 |
| Chain | Residue | Details |
| A | PHE215 | |
| B | PHE215 | |
| C | PHE215 | |
| D | PHE215 | |
| E | PHE215 | |
| F | PHE215 |
