2QQC
E109Q mutant 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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | L-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 | 7 |
| Details | BINDING SITE FOR RESIDUE AG2 A 671 |
| Chain | Residue |
| A | SER52 |
| B | ILE107 |
| B | GLN109 |
| C | LEU31 |
| C | ASP35 |
| C | LEU38 |
| C | GLY44 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AG2 E 671 |
| Chain | Residue |
| D | GLN109 |
| D | ARG134 |
| E | LEU31 |
| E | ASP35 |
| E | LEU38 |
| E | GLY44 |
| C | SER52 |
| D | ILE107 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AG2 A 672 |
| Chain | Residue |
| A | LEU31 |
| A | ASP35 |
| A | LEU38 |
| A | GLY44 |
| E | SER52 |
| F | ILE107 |
| F | MET108 |
| F | GLN109 |
| F | ARG134 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE AG2 K 671 |
| Chain | Residue |
| G | SER52 |
| H | ILE107 |
| H | MET108 |
| H | GLN109 |
| H | ARG134 |
| K | LEU31 |
| K | ASP35 |
| K | LEU38 |
| K | GLY44 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AG2 I 671 |
| Chain | Residue |
| G | LEU31 |
| G | ASP35 |
| G | LEU38 |
| G | GLY44 |
| I | SER52 |
| J | ILE107 |
| J | GLN109 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AG2 I 672 |
| Chain | Residue |
| I | LEU31 |
| I | ASP35 |
| I | LEU38 |
| I | GLY44 |
| K | SER52 |
| L | ILE107 |
| L | MET108 |
| L | GLN109 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR B 53 |
| Chain | Residue |
| A | ILE51 |
| B | ILE54 |
| B | ALA76 |
| B | LEU106 |
| B | ILE107 |
| C | ASN47 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR D 53 |
| Chain | Residue |
| C | ILE51 |
| D | ILE54 |
| D | ALA76 |
| D | LEU106 |
| D | ILE107 |
| E | ASN47 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR F 53 |
| Chain | Residue |
| A | ASN47 |
| E | ILE51 |
| F | ILE54 |
| F | ALA76 |
| F | LEU106 |
| F | ILE107 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PYR H 53 |
| Chain | Residue |
| G | ILE51 |
| H | ILE54 |
| H | LEU106 |
| H | ILE107 |
| K | ASN47 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PYR J 53 |
| Chain | Residue |
| G | ASN47 |
| I | ILE51 |
| J | ILE54 |
| J | ILE107 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PYR L 53 |
| Chain | Residue |
| I | ASN47 |
| K | ILE51 |
| L | ILE54 |
| L | ALA76 |
| L | LEU106 |
| L | ILE107 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD C 700 |
| Chain | Residue |
| C | LEU31 |
| C | PHE34 |
| D | TYR77 |
| D | TYR79 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD E 700 |
| Chain | Residue |
| C | HOH716 |
| E | LEU31 |
| E | PHE34 |
| F | TYR79 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 700 |
| Chain | Residue |
| A | LEU31 |
| B | TYR77 |
| B | TYR79 |
| E | HOH750 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MPD I 700 |
| Chain | Residue |
| I | PHE34 |
| K | HOH697 |
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 | LYS113 | proton shuttle (general acid/base) |
| A | SER52 |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| D | LYS113 | proton shuttle (general acid/base) |
| C | SER52 |
| site_id | MCSA3 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| F | LYS113 | proton shuttle (general acid/base) |
| E | SER52 |
| site_id | MCSA4 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| H | LYS113 | proton shuttle (general acid/base) |
| G | SER52 |
| site_id | MCSA5 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| J | LYS113 | proton shuttle (general acid/base) |
| I | SER52 |
| site_id | MCSA6 |
| Number of Residues | 1 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| L | LYS113 | proton shuttle (general acid/base) |
| K | SER52 |
