1XEY
Crystal structure of the complex of Escherichia coli GADA with glutarate at 2.05 A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004351 | molecular_function | glutamate decarboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0006538 | biological_process | glutamate catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016830 | molecular_function | carbon-carbon lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0051454 | biological_process | intracellular pH elevation |
| B | 0004351 | molecular_function | glutamate decarboxylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0006538 | biological_process | glutamate catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016830 | molecular_function | carbon-carbon lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019752 | biological_process | carboxylic acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0051454 | biological_process | intracellular pH elevation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 600 |
| Chain | Residue |
| A | LEU279 |
| A | LEU334 |
| A | VAL342 |
| A | ARG427 |
| A | HOH859 |
| B | SER16 |
| B | HOH858 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 700 |
| Chain | Residue |
| A | PHE18 |
| A | HOH714 |
| B | TRP67 |
| B | VAL342 |
| B | ARG427 |
| A | SER16 |
| A | ARG17 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | SER126 |
| A | SER127 |
| A | GLN163 |
| A | CYS165 |
| A | THR208 |
| A | THR212 |
| A | ASP243 |
| A | ALA245 |
| A | SER273 |
| A | HIS275 |
| A | LYS276 |
| A | HOH738 |
| A | HOH784 |
| B | PHE317 |
| B | SER318 |
| B | GUA505 |
| B | HOH959 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| A | PHE317 |
| A | SER318 |
| A | GUA506 |
| B | GLY125 |
| B | SER126 |
| B | SER127 |
| B | GLN163 |
| B | CYS165 |
| B | THR208 |
| B | THR212 |
| B | ASP243 |
| B | ALA245 |
| B | SER273 |
| B | HIS275 |
| B | LYS276 |
| B | HOH826 |
| B | HOH879 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GUA B 505 |
| Chain | Residue |
| A | THR62 |
| A | PHE63 |
| A | GLN163 |
| A | LYS276 |
| A | ARG422 |
| A | PLP500 |
| B | ASN83 |
| B | ASP86 |
| B | GLU89 |
| B | HOH959 |
| B | HOH1074 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GUA A 506 |
| Chain | Residue |
| A | ASN83 |
| A | ASP86 |
| A | GLU89 |
| B | THR62 |
| B | PHE63 |
| B | GLN163 |
| B | LYS276 |
| B | PLP500 |
Functional Information from PROSITE/UniProt
| site_id | PS00392 |
| Number of Residues | 22 |
| Details | DDC_GAD_HDC_YDC DDC / GAD / HDC / TyrDC pyridoxal-phosphate attachment site. SIsAsghKFGlApLGCgwVIwR |
| Chain | Residue | Details |
| A | SER269-ARG290 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | THR62 | |
| B | HIS275 | |
| A | ASN83 | |
| A | SER126 | |
| A | THR212 | |
| A | HIS275 | |
| B | THR62 | |
| B | ASN83 | |
| B | SER126 | |
| B | THR212 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS276 | |
| B | LYS276 |
