Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001081 | biological_process | nitrogen catabolite repression of transcription from RNA polymerase II promoter |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0006808 | biological_process | regulation of nitrogen utilization |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0051287 | molecular_function | NAD binding |
A | 0070401 | molecular_function | NADP+ binding |
A | 0070402 | molecular_function | NADPH binding |
A | 0070403 | molecular_function | NAD+ binding |
A | 0070404 | molecular_function | NADH binding |
A | 0070405 | molecular_function | ammonium ion binding |
A | 0070406 | molecular_function | glutamine binding |
A | 0090295 | biological_process | nitrogen catabolite repression of transcription |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 379 |
Chain | Residue |
A | GLN48 |
A | ILE50 |
A | VAL53 |
A | HOH1150 |
A | HOH1481 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 380 |
Chain | Residue |
A | SER145 |
A | HOH1035 |
A | VAL138 |
A | ARG139 |
A | LEU141 |
A | LEU143 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K A 381 |
Chain | Residue |
A | SER111 |
A | SER112 |
A | MET113 |
A | VAL148 |
A | ALA150 |
A | HOH1193 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K A 382 |
Chain | Residue |
A | SER117 |
A | GLY120 |
A | HOH1155 |
A | HOH1413 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K A 383 |
Chain | Residue |
A | GLN140 |
A | GLY347 |
A | ASP349 |
A | HOH1109 |
A | HOH1118 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 384 |
Chain | Residue |
A | GLN106 |
A | PRO208 |
A | VAL252 |
A | ASN253 |
A | HOH1069 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 385 |
Chain | Residue |
A | LYS6 |
A | HIS30 |
A | ASN253 |
A | HOH1051 |
A | HOH1333 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 386 |
Chain | Residue |
A | GLN166 |
A | GLU168 |
A | LYS251 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 387 |
Chain | Residue |
A | TYR276 |
A | PHE277 |
A | HOH1253 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 388 |
Chain | Residue |
A | THR241 |
A | TYR242 |
A | HOH1229 |
A | HOH1334 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 389 |
Chain | Residue |
A | ASN12 |
A | THR14 |
A | VAL36 |
A | HIS37 |
A | HOH1166 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 390 |
Chain | Residue |
A | ARG33 |
A | HOH1443 |
site_id | BC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 391 |
Chain | Residue |
A | LEU169 |
A | ASP349 |
A | TRP350 |
A | HOH1226 |
A | HOH1301 |
site_id | BC5 |
Number of Residues | 27 |
Details | BINDING SITE FOR RESIDUE NAP A 400 |
Chain | Residue |
A | ASN12 |
A | THR14 |
A | GLY15 |
A | ARG16 |
A | GLN17 |
A | HIS37 |
A | ASN80 |
A | THR81 |
A | THR82 |
A | GLN84 |
A | ALA85 |
A | MET113 |
A | LYS131 |
A | ALA150 |
A | GLY151 |
A | ILE152 |
A | TYR153 |
A | ASN156 |
A | TYR276 |
A | HOH1141 |
A | HOH1167 |
A | HOH1169 |
A | HOH1171 |
A | HOH1189 |
A | HOH1190 |
A | HOH1199 |
A | HOH1465 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 392 |
Chain | Residue |
A | PRO198 |
A | LEU201 |
A | GLN202 |
A | LYS205 |
A | LEU324 |
A | TRP325 |
A | GLU344 |
A | HOH1130 |
A | HOH1287 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN12 | |
A | HIS37 | |
A | ASN80 | |
A | LYS131 | |
A | TYR153 | |
Chain | Residue | Details |
A | ARG16 | |