2DGL
Crystal structure of Escherichia coli GadB in complex with bromide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004351 | molecular_function | glutamate decarboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006536 | biological_process | glutamate metabolic process |
| A | 0006538 | biological_process | L-glutamate catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| 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 | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006536 | biological_process | glutamate metabolic process |
| B | 0006538 | biological_process | L-glutamate catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| 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 |
| C | 0004351 | molecular_function | glutamate decarboxylase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006536 | biological_process | glutamate metabolic process |
| C | 0006538 | biological_process | L-glutamate catabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016830 | molecular_function | carbon-carbon lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019752 | biological_process | carboxylic acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0051454 | biological_process | intracellular pH elevation |
| D | 0004351 | molecular_function | glutamate decarboxylase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006536 | biological_process | glutamate metabolic process |
| D | 0006538 | biological_process | L-glutamate catabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016830 | molecular_function | carbon-carbon lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019752 | biological_process | carboxylic acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0051454 | biological_process | intracellular pH elevation |
| E | 0004351 | molecular_function | glutamate decarboxylase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006536 | biological_process | glutamate metabolic process |
| E | 0006538 | biological_process | L-glutamate catabolic process |
| E | 0016020 | cellular_component | membrane |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016830 | molecular_function | carbon-carbon lyase activity |
| E | 0016831 | molecular_function | carboxy-lyase activity |
| E | 0019752 | biological_process | carboxylic acid metabolic process |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0051454 | biological_process | intracellular pH elevation |
| F | 0004351 | molecular_function | glutamate decarboxylase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0006536 | biological_process | glutamate metabolic process |
| F | 0006538 | biological_process | L-glutamate catabolic process |
| F | 0016020 | cellular_component | membrane |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016830 | molecular_function | carbon-carbon lyase activity |
| F | 0016831 | molecular_function | carboxy-lyase activity |
| F | 0019752 | biological_process | carboxylic acid metabolic process |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0051454 | biological_process | intracellular pH elevation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR A 467 |
| Chain | Residue |
| A | SER16 |
| F | ARG427 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR F 467 |
| Chain | Residue |
| E | ASN81 |
| F | ASP68 |
| F | HIS73 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 468 |
| Chain | Residue |
| A | ARG17 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 467 |
| Chain | Residue |
| B | SER16 |
| C | ARG427 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR C 467 |
| Chain | Residue |
| C | ASP68 |
| C | HIS73 |
| C | TRP67 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR B 468 |
| Chain | Residue |
| B | ARG17 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 469 |
| Chain | Residue |
| B | ARG427 |
| C | SER16 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR B 470 |
| Chain | Residue |
| A | ASN81 |
| B | ASP68 |
| B | HIS73 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR C 468 |
| Chain | Residue |
| C | ARG17 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR D 467 |
| Chain | Residue |
| D | SER16 |
| E | ARG427 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR E 467 |
| Chain | Residue |
| E | ASP68 |
| E | HIS73 |
| F | ASN81 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR D 468 |
| Chain | Residue |
| D | ARG17 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR E 468 |
| Chain | Residue |
| D | ARG427 |
| E | SER16 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR C 469 |
| Chain | Residue |
| C | ASN81 |
| D | ASP68 |
| D | HIS73 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR E 469 |
| Chain | Residue |
| E | ARG17 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR F 468 |
| Chain | Residue |
| A | ARG427 |
| F | SER16 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BR A 469 |
| Chain | Residue |
| A | ASP68 |
| A | HIS73 |
| B | ASN81 |
| site_id | BC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR F 469 |
| Chain | Residue |
| F | ARG17 |
| site_id | CC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR A 470 |
| Chain | Residue |
| A | ILE418 |
| site_id | CC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR B 471 |
| Chain | Residue |
| B | LYS381 |
| B | ILE418 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BR C 470 |
| Chain | Residue |
| C | LYS381 |
| C | ILE418 |
| site_id | CC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR D 469 |
| Chain | Residue |
| D | LYS381 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BR E 470 |
| Chain | Residue |
| E | ILE418 |
| site_id | CC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | GLY125 |
| A | SER126 |
| A | SER127 |
| A | GLN163 |
| A | THR212 |
| A | ASP243 |
| A | ALA245 |
| A | SER273 |
| A | HIS275 |
| A | LYS276 |
| B | PHE317 |
| B | SER318 |
| site_id | CC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| A | PHE317 |
| A | SER318 |
| B | GLY125 |
| B | SER126 |
| B | SER127 |
| B | GLN163 |
| B | THR212 |
| B | ASP243 |
| B | ALA245 |
| B | SER273 |
| B | HIS275 |
| B | LYS276 |
| B | HOH567 |
| site_id | CC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP C 501 |
| Chain | Residue |
| C | GLY125 |
| C | SER126 |
| C | SER127 |
| C | GLN163 |
| C | THR212 |
| C | ASP243 |
| C | ALA245 |
| C | SER273 |
| C | HIS275 |
| C | LYS276 |
| D | PHE317 |
| D | SER318 |
| site_id | CC9 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP D 501 |
| Chain | Residue |
| C | PHE317 |
| C | SER318 |
| D | SER126 |
| D | SER127 |
| D | GLN163 |
| D | CYS165 |
| D | THR212 |
| D | ASP243 |
| D | ALA245 |
| D | SER273 |
| D | HIS275 |
| D | LYS276 |
| site_id | DC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP E 502 |
| Chain | Residue |
| E | ALA245 |
| E | SER273 |
| E | HIS275 |
| E | LYS276 |
| F | PHE317 |
| F | SER318 |
| E | GLY125 |
| E | SER126 |
| E | SER127 |
| E | GLN163 |
| E | CYS165 |
| E | THR212 |
| E | ASP243 |
| site_id | DC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP F 502 |
| Chain | Residue |
| E | PHE317 |
| E | SER318 |
| E | HOH529 |
| F | GLY125 |
| F | SER126 |
| F | SER127 |
| F | GLN163 |
| F | THR208 |
| F | THR212 |
| F | ASP243 |
| F | ALA245 |
| F | SER273 |
| F | HIS275 |
| F | LYS276 |
| site_id | DC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACY E 518 |
| Chain | Residue |
| E | THR62 |
| E | PHE63 |
| F | ASP86 |
| site_id | DC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY F 528 |
| Chain | Residue |
| E | ASN83 |
| E | ASP86 |
| E | SER318 |
| F | THR62 |
| F | PHE63 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY C 538 |
| Chain | Residue |
| C | THR62 |
| C | PHE63 |
| D | ASP86 |
| D | SER318 |
| site_id | DC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY C 548 |
| Chain | Residue |
| C | ASN83 |
| C | ASP86 |
| C | PHE317 |
| C | SER318 |
| D | THR62 |
| D | PHE63 |
| D | CYS64 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 558 |
| Chain | Residue |
| A | THR62 |
| A | PHE63 |
| A | CYS64 |
| B | ASN83 |
| B | ASP86 |
| site_id | DC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 568 |
| Chain | Residue |
| A | ASN83 |
| A | ASP86 |
| A | SER318 |
| B | THR62 |
| B | PHE63 |
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 | 30 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
