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 | 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 | 0030234 | molecular_function | enzyme regulator activity |
G | 0042802 | molecular_function | identical protein binding |
G | 0045848 | biological_process | positive regulation of nitrogen utilization |
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 | 0030234 | molecular_function | enzyme regulator activity |
H | 0042802 | molecular_function | identical protein binding |
H | 0045848 | biological_process | positive regulation of nitrogen utilization |
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 | 0030234 | molecular_function | enzyme regulator activity |
I | 0042802 | molecular_function | identical protein binding |
I | 0045848 | biological_process | positive regulation of nitrogen utilization |
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 | 0030234 | molecular_function | enzyme regulator activity |
J | 0042802 | molecular_function | identical protein binding |
J | 0045848 | biological_process | positive regulation of nitrogen utilization |
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 | 0030234 | molecular_function | enzyme regulator activity |
K | 0042802 | molecular_function | identical protein binding |
K | 0045848 | biological_process | positive regulation of nitrogen utilization |
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 | 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 |
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 | |
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 | |
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 | |
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 | |
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 | |
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 | |
G | THR29 | |
H | THR29 | |
I | THR29 | |
J | THR29 | |
K | THR29 | |
L | THR29 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9733647, ECO:0007744|PDB:2GNK |
Chain | Residue | Details |
F | GLU121-ARG124 | |
E | THR300-PRO311 | |
F | GLY33-SER43 | |
F | TYR180-PRO199 | |
F | LEU252-SER257 | |
F | THR300-PRO311 | |
G | GLY37 | |
G | ALA64 | |
G | GLY87 | |
G | ARG101 | |
H | GLY37 | |
H | ALA64 | |
H | GLY87 | |
H | ARG101 | |
I | GLY37 | |
I | ALA64 | |
I | GLY87 | |
I | ARG101 | |
J | GLY37 | |
J | ALA64 | |
J | GLY87 | |
J | ARG101 | |
K | GLY37 | |
K | ALA64 | |
K | GLY87 | |
K | ARG101 | |
L | GLY37 | |
L | ALA64 | |
L | GLY87 | |
L | ARG101 |
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 |
B | GLY150-GLY163 | |
B | ALA220-ILE226 | |
B | ILE279-GLY280 | |
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 | |
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 | |
F | ALA334-MET348 | |
G | ARG38 | |
H | ARG38 | |
I | ARG38 | |
J | ARG38 | |
K | ARG38 | |
L | ARG38 |
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 | |
A | HIS318 | |
B | HIS168 | |
B | HIS318 | |
C | HIS168 | |
C | HIS318 | |
D | HIS168 | |
D | HIS318 | |
E | HIS168 | |
E | HIS318 | |
F | HIS168 | |
F | HIS318 |
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 |