3N2O
X-ray crystal structure of arginine decarboxylase complexed with Arginine from Vibrio vulnificus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0006527 | biological_process | L-arginine catabolic process |
| A | 0006596 | biological_process | polyamine biosynthetic process |
| A | 0008295 | biological_process | spermidine biosynthetic process |
| A | 0008792 | molecular_function | arginine decarboxylase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0006527 | biological_process | L-arginine catabolic process |
| B | 0006596 | biological_process | polyamine biosynthetic process |
| B | 0008295 | biological_process | spermidine biosynthetic process |
| B | 0008792 | molecular_function | arginine decarboxylase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0006527 | biological_process | L-arginine catabolic process |
| C | 0006596 | biological_process | polyamine biosynthetic process |
| C | 0008295 | biological_process | spermidine biosynthetic process |
| C | 0008792 | molecular_function | arginine decarboxylase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0006527 | biological_process | L-arginine catabolic process |
| D | 0006596 | biological_process | polyamine biosynthetic process |
| D | 0008295 | biological_process | spermidine biosynthetic process |
| D | 0008792 | molecular_function | arginine decarboxylase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0033388 | biological_process | putrescine biosynthetic process from arginine |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP A 1001 |
| Chain | Residue |
| A | PRO103 |
| A | GLY345 |
| A | ARG346 |
| A | TYR551 |
| A | HOH649 |
| A | HOH698 |
| A | HOH699 |
| A | LYS105 |
| A | ASN155 |
| A | HIS255 |
| A | SER258 |
| A | GLY294 |
| A | GLY295 |
| A | GLU343 |
| A | SER344 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AG2 A 1002 |
| Chain | Residue |
| A | TRP482 |
| A | ASP512 |
| A | SER513 |
| B | LYS105 |
| B | HIS255 |
| B | GLY257 |
| B | SER258 |
| B | ASP480 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AG2 B 1002 |
| Chain | Residue |
| A | LYS105 |
| A | HIS255 |
| A | GLY257 |
| A | SER258 |
| B | ASP512 |
| B | SER513 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 1001 |
| Chain | Residue |
| A | CYS511 |
| B | LYS105 |
| B | GLU131 |
| B | HIS255 |
| B | SER258 |
| B | GLY294 |
| B | GLY295 |
| B | GLU343 |
| B | GLY345 |
| B | ARG346 |
| B | TYR551 |
| B | HOH654 |
| B | HOH656 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP C 1001 |
| Chain | Residue |
| C | PRO103 |
| C | LYS105 |
| C | GLU131 |
| C | HIS255 |
| C | SER258 |
| C | GLY294 |
| C | GLY295 |
| C | GLU343 |
| C | GLY345 |
| C | ARG346 |
| C | TYR551 |
| C | HOH649 |
| C | HOH651 |
| C | HOH742 |
| D | CYS511 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AG2 C 1002 |
| Chain | Residue |
| C | LYS105 |
| C | HIS255 |
| C | ASP480 |
| C | LEU555 |
| D | ASP512 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PLP D 1001 |
| Chain | Residue |
| D | LYS105 |
| D | ASN155 |
| D | HIS255 |
| D | SER258 |
| D | GLY294 |
| D | GLY295 |
| D | GLU343 |
| D | GLY345 |
| D | ARG346 |
| D | TYR551 |
| D | HOH673 |
| D | HOH737 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AG2 D 1002 |
| Chain | Residue |
| C | ASP512 |
| D | HIS255 |
| D | SER258 |
| D | ARG346 |
| D | ASP480 |
| D | LEU555 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01417","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01417","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
