4NH2
Crystal structure of AmtB from E. coli bound to phosphatidylglycerol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008519 | molecular_function | ammonium channel activity |
| A | 0016020 | cellular_component | membrane |
| A | 0072488 | biological_process | ammonium transmembrane transport |
| B | 0008519 | molecular_function | ammonium channel activity |
| B | 0016020 | cellular_component | membrane |
| B | 0072488 | biological_process | ammonium transmembrane transport |
| C | 0008519 | molecular_function | ammonium channel activity |
| C | 0016020 | cellular_component | membrane |
| C | 0072488 | biological_process | ammonium transmembrane transport |
| D | 0008519 | molecular_function | ammonium channel activity |
| D | 0016020 | cellular_component | membrane |
| D | 0072488 | biological_process | ammonium transmembrane transport |
| E | 0008519 | molecular_function | ammonium channel activity |
| E | 0016020 | cellular_component | membrane |
| E | 0072488 | biological_process | ammonium transmembrane transport |
| F | 0008519 | molecular_function | ammonium channel activity |
| F | 0016020 | cellular_component | membrane |
| F | 0072488 | biological_process | ammonium transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE P6L A 501 |
| Chain | Residue |
| A | ASN72 |
| C | GLY349 |
| C | LEU352 |
| A | PHE75 |
| A | GLY76 |
| A | ASN77 |
| A | ILE78 |
| A | ASN79 |
| A | HOH616 |
| C | THR347 |
| C | MET348 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE P6L B 501 |
| Chain | Residue |
| B | ASN72 |
| B | PHE75 |
| B | ASN79 |
| B | HOH609 |
| D | THR347 |
| D | MET348 |
| D | GLY349 |
| D | LEU352 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE P6L C 501 |
| Chain | Residue |
| C | VAL61 |
| C | LEU66 |
| C | GLU70 |
| C | ASN72 |
| C | PHE75 |
| C | GLY76 |
| C | ILE78 |
| C | HOH610 |
| F | THR347 |
| F | MET348 |
| F | GLY349 |
| F | LEU352 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE P6L C 502 |
| Chain | Residue |
| A | TRP80 |
| A | LYS84 |
| B | LYS84 |
| C | GLY282 |
| C | GLY283 |
| C | ILE286 |
| C | SER335 |
| C | SER336 |
| C | LEU337 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE P6L D 501 |
| Chain | Residue |
| D | LEU66 |
| D | ASN72 |
| D | PHE75 |
| D | ILE78 |
| D | LEU138 |
| D | HOH604 |
| E | THR347 |
| E | MET348 |
| E | GLY349 |
| E | LEU352 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE P6L E 501 |
| Chain | Residue |
| A | GLY349 |
| A | LEU352 |
| E | LEU66 |
| E | GLY71 |
| E | ASN72 |
| E | PHE75 |
| E | ASN77 |
| E | ILE78 |
| E | THR137 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE P6L F 501 |
| Chain | Residue |
| B | THR347 |
| B | MET348 |
| B | GLY349 |
| B | LEU352 |
| F | GLY71 |
| F | ASN72 |
| F | PHE75 |
| F | GLY76 |
| F | ILE78 |
| F | THR137 |
| F | HOH615 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE P6L F 502 |
| Chain | Residue |
| B | LEU285 |
| B | ILE286 |
| B | VAL289 |
| B | PHE332 |
| E | LYS84 |
| F | LEU81 |
| F | LYS84 |
| F | HOH610 |
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 |
