1N13
The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| 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 |
| K | 0006520 | biological_process | amino acid metabolic process |
| K | 0006527 | biological_process | arginine catabolic process |
| K | 0008792 | molecular_function | arginine decarboxylase activity |
| K | 0016831 | molecular_function | carboxy-lyase activity |
| L | 0006520 | biological_process | amino acid metabolic process |
| L | 0006527 | biological_process | arginine catabolic process |
| L | 0008792 | molecular_function | arginine decarboxylase activity |
| L | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AG2 B 7011 |
| Chain | Residue |
| A | SER52 |
| C | VAL46 |
| A | HOH6663 |
| B | PYR53 |
| B | ILE107 |
| B | GLU109 |
| C | LEU31 |
| C | ASP35 |
| C | LEU38 |
| C | GLY44 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AG2 H 7012 |
| Chain | Residue |
| G | SER52 |
| G | HOH6664 |
| H | PYR53 |
| H | ILE107 |
| H | GLU109 |
| K | LEU31 |
| K | ASP35 |
| K | LEU38 |
| K | GLY44 |
| K | VAL46 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE AG2 J 7013 |
| Chain | Residue |
| G | LEU31 |
| G | ASP35 |
| G | LEU38 |
| G | GLY44 |
| G | VAL46 |
| H | HOH6654 |
| I | SER52 |
| J | PYR53 |
| J | ILE107 |
| J | GLU109 |
| J | HOH6659 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE AG2 L 7014 |
| Chain | Residue |
| I | LEU31 |
| I | ASP35 |
| I | LEU38 |
| I | GLY44 |
| I | VAL46 |
| J | HOH6662 |
| K | SER52 |
| L | PYR53 |
| L | ILE107 |
| L | MET108 |
| L | GLU109 |
| L | HOH6658 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AG2 D 7015 |
| Chain | Residue |
| C | SER52 |
| D | PYR53 |
| D | ILE107 |
| D | GLU109 |
| D | HOH6661 |
| E | LEU31 |
| E | ASP35 |
| E | LEU38 |
| E | GLY44 |
| E | VAL46 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE AG2 F 7016 |
| Chain | Residue |
| A | PHE34 |
| A | ASP35 |
| A | LEU38 |
| A | GLY44 |
| A | VAL46 |
| E | SER52 |
| F | PYR53 |
| F | ILE107 |
| F | GLU109 |
| F | HOH6655 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MRD D 7001 |
| Chain | Residue |
| D | TYR77 |
| D | TYR79 |
| D | HOH6656 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD L 7002 |
| Chain | Residue |
| G | HOH6660 |
| K | LEU31 |
| L | TYR77 |
| L | TYR79 |
| L | ILE81 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD H 7003 |
| Chain | Residue |
| G | LEU31 |
| G | PHE34 |
| H | TYR77 |
| H | TYR79 |
| H | HOH6654 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD J 7004 |
| Chain | Residue |
| I | LEU31 |
| J | TYR77 |
| J | TYR79 |
| J | ILE81 |
| J | HOH6662 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD F 7005 |
| Chain | Residue |
| E | LEU31 |
| E | PHE34 |
| F | TYR77 |
| F | TYR79 |
| F | ILE81 |
| F | HOH6020 |
| F | HOH6673 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD B 7006 |
| Chain | Residue |
| A | LEU31 |
| A | PHE34 |
| B | TYR77 |
| B | TYR79 |
| B | ILE81 |
| B | HOH6653 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD H 7007 |
| Chain | Residue |
| L | GLU137 |
| L | HOH6330 |
| H | GLU132 |
| H | GLY135 |
| H | TRP136 |
| L | GLY135 |
| L | TRP136 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD D 7008 |
| Chain | Residue |
| D | GLU132 |
| D | GLY135 |
| D | TRP136 |
| F | GLY135 |
| F | TRP136 |
| F | HOH6290 |
| F | HOH6320 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | SITE: Cleavage (non-hydrolytic) |
| Chain | Residue | Details |
| A | SER52 | |
| C | SER52 | |
| E | SER52 | |
| G | SER52 | |
| I | SER52 | |
| K | SER52 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| B | GLU109 | proton shuttle (general acid/base) |
| A | SER52 |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| D | GLU109 | proton shuttle (general acid/base) |
| C | SER52 |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| F | GLU109 | proton shuttle (general acid/base) |
| E | SER52 |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| H | GLU109 | proton shuttle (general acid/base) |
| G | SER52 |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| J | GLU109 | proton shuttle (general acid/base) |
| I | SER52 |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| L | GLU109 | proton shuttle (general acid/base) |
| K | SER52 |
