2VYC
Crystal Structure of Acid Induced Arginine Decarboxylase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006527 | biological_process | arginine catabolic process |
| A | 0008792 | molecular_function | arginine decarboxylase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0051454 | biological_process | intracellular pH elevation |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006527 | biological_process | arginine catabolic process |
| B | 0008792 | molecular_function | arginine decarboxylase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0051454 | biological_process | intracellular pH elevation |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006527 | biological_process | arginine catabolic process |
| C | 0008792 | molecular_function | arginine decarboxylase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0051454 | biological_process | intracellular pH elevation |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006527 | biological_process | arginine catabolic process |
| D | 0008792 | molecular_function | arginine decarboxylase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0051454 | biological_process | intracellular pH elevation |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006520 | biological_process | amino acid metabolic process |
| E | 0006527 | biological_process | arginine catabolic process |
| E | 0008792 | molecular_function | arginine decarboxylase activity |
| E | 0016831 | molecular_function | carboxy-lyase activity |
| E | 0030170 | molecular_function | pyridoxal phosphate binding |
| E | 0051454 | biological_process | intracellular pH elevation |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0006520 | biological_process | amino acid metabolic process |
| F | 0006527 | biological_process | arginine catabolic process |
| F | 0008792 | molecular_function | arginine decarboxylase activity |
| F | 0016831 | molecular_function | carboxy-lyase activity |
| F | 0030170 | molecular_function | pyridoxal phosphate binding |
| F | 0051454 | biological_process | intracellular pH elevation |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0006520 | biological_process | amino acid metabolic process |
| G | 0006527 | biological_process | arginine catabolic process |
| G | 0008792 | molecular_function | arginine decarboxylase activity |
| G | 0016831 | molecular_function | carboxy-lyase activity |
| G | 0030170 | molecular_function | pyridoxal phosphate binding |
| G | 0051454 | biological_process | intracellular pH elevation |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0006520 | biological_process | amino acid metabolic process |
| H | 0006527 | biological_process | arginine catabolic process |
| H | 0008792 | molecular_function | arginine decarboxylase activity |
| H | 0016831 | molecular_function | carboxy-lyase activity |
| H | 0030170 | molecular_function | pyridoxal phosphate binding |
| H | 0051454 | biological_process | intracellular pH elevation |
| I | 0003824 | molecular_function | catalytic activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0005829 | cellular_component | cytosol |
| I | 0006520 | biological_process | amino acid metabolic process |
| I | 0006527 | biological_process | arginine catabolic process |
| I | 0008792 | molecular_function | arginine decarboxylase activity |
| I | 0016831 | molecular_function | carboxy-lyase activity |
| I | 0030170 | molecular_function | pyridoxal phosphate binding |
| I | 0051454 | biological_process | intracellular pH elevation |
| J | 0003824 | molecular_function | catalytic activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0005829 | cellular_component | cytosol |
| J | 0006520 | biological_process | amino acid metabolic process |
| J | 0006527 | biological_process | arginine catabolic process |
| J | 0008792 | molecular_function | arginine decarboxylase activity |
| J | 0016831 | molecular_function | carboxy-lyase activity |
| J | 0030170 | molecular_function | pyridoxal phosphate binding |
| J | 0051454 | biological_process | intracellular pH elevation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1386 |
| Chain | Residue |
| A | GLY229 |
| A | SER383 |
| A | HIS385 |
| A | LYS386 |
| C | THR420 |
| C | THR421 |
| C | SER422 |
| A | THR230 |
| A | SER231 |
| A | ASN234 |
| A | HIS255 |
| A | SER257 |
| A | ASP347 |
| A | ALA349 |
| A | TRP350 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP B 1386 |
| Chain | Residue |
| B | GLY229 |
| B | THR230 |
| B | SER231 |
| B | ASN234 |
| B | HIS255 |
| B | ASP347 |
| B | ALA349 |
| B | TRP350 |
| B | SER383 |
| B | HIS385 |
| B | LYS386 |
| B | THR420 |
| B | THR421 |
| B | SER422 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP C 1386 |
| Chain | Residue |
| A | THR420 |
| A | THR421 |
| A | SER422 |
| C | GLY229 |
| C | THR230 |
| C | SER231 |
| C | ASN234 |
| C | HIS255 |
| C | ASP347 |
| C | ALA349 |
| C | TRP350 |
| C | SER383 |
| C | HIS385 |
| C | LYS386 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP D 1386 |
| Chain | Residue |
| D | GLY229 |
| D | THR230 |
| D | SER231 |
| D | ASN234 |
| D | HIS255 |
| D | ASP347 |
| D | ALA349 |
| D | TRP350 |
| D | SER383 |
| D | HIS385 |
| D | LYS386 |
| E | THR420 |
| E | THR421 |
| E | SER422 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP E 1386 |
| Chain | Residue |
| D | THR420 |
| D | THR421 |
| D | SER422 |
| E | GLY229 |
| E | THR230 |
| E | SER231 |
| E | HIS255 |
| E | ASP347 |
| E | ALA349 |
| E | TRP350 |
| E | SER383 |
| E | HIS385 |
| E | LYS386 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP F 1386 |
| Chain | Residue |
| F | GLY229 |
| F | THR230 |
| F | SER231 |
| F | ASN234 |
| F | HIS255 |
| F | ASP347 |
| F | ALA349 |
| F | TRP350 |
| F | SER383 |
| F | HIS385 |
| F | LYS386 |
| F | THR420 |
| F | THR421 |
| F | SER422 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP G 1386 |
| Chain | Residue |
| G | GLY229 |
| G | THR230 |
| G | SER231 |
| G | ASN234 |
| G | HIS255 |
| G | ASP347 |
| G | ALA349 |
| G | TRP350 |
| G | SER383 |
| G | HIS385 |
| G | LYS386 |
| J | THR420 |
| J | THR421 |
| J | SER422 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP H 1386 |
| Chain | Residue |
| H | THR230 |
| H | SER231 |
| H | ASN234 |
| H | HIS255 |
| H | ASP347 |
| H | ALA349 |
| H | TRP350 |
| H | SER383 |
| H | HIS385 |
| H | LYS386 |
| I | THR420 |
| I | THR421 |
| I | SER422 |
| H | GLY229 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP I 1386 |
| Chain | Residue |
| H | THR420 |
| H | THR421 |
| H | SER422 |
| I | GLY229 |
| I | THR230 |
| I | SER231 |
| I | HIS255 |
| I | ASP347 |
| I | ALA349 |
| I | TRP350 |
| I | SER383 |
| I | HIS385 |
| I | LYS386 |
| site_id | BC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PLP J 1386 |
| Chain | Residue |
| G | THR420 |
| G | THR421 |
| G | SER422 |
| J | GLY229 |
| J | THR230 |
| J | SER231 |
| J | ASN234 |
| J | HIS255 |
| J | ASP347 |
| J | ALA349 |
| J | TRP350 |
| J | SER383 |
| J | HIS385 |
| J | LYS386 |
Functional Information from PROSITE/UniProt
| site_id | PS00703 |
| Number of Residues | 15 |
| Details | OKR_DC_1 Orn/Lys/Arg decarboxylases family 1 pyridoxal-P attachment site. ThStHKllNAlSQAS |
| Chain | Residue | Details |
| A | THR381-SER395 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:19298070, ECO:0007744|PDB:2VYC |
| Chain | Residue | Details |
| A | LYS386 | |
| J | LYS386 | |
| B | LYS386 | |
| C | LYS386 | |
| D | LYS386 | |
| E | LYS386 | |
| F | LYS386 | |
| G | LYS386 | |
| H | LYS386 | |
| I | LYS386 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | SER383 | |
| A | GLU183 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| J | SER383 | |
| J | GLU183 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| A | ASP347 | |
| A | HIS255 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | ASP347 | |
| B | HIS255 |
| site_id | CSA13 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| C | ASP347 | |
| C | HIS255 |
| site_id | CSA14 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| D | ASP347 | |
| D | HIS255 |
| site_id | CSA15 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| E | ASP347 | |
| E | HIS255 |
| site_id | CSA16 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| F | ASP347 | |
| F | HIS255 |
| site_id | CSA17 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| G | ASP347 | |
| G | HIS255 |
| site_id | CSA18 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| H | ASP347 | |
| H | HIS255 |
| site_id | CSA19 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| I | ASP347 | |
| I | HIS255 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| B | SER383 | |
| B | GLU183 |
| site_id | CSA20 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| J | ASP347 | |
| J | HIS255 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| C | SER383 | |
| C | GLU183 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| D | SER383 | |
| D | GLU183 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| E | SER383 | |
| E | GLU183 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| F | SER383 | |
| F | GLU183 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| G | SER383 | |
| G | GLU183 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| H | SER383 | |
| H | GLU183 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dfo |
| Chain | Residue | Details |
| I | SER383 | |
| I | GLU183 |
