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 |