1N2M
The S53A Proenzyme Structure of Methanococcus jannaschii.
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 | 0016829 | molecular_function | lyase 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 | 0016829 | molecular_function | lyase 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 | 0016829 | molecular_function | lyase 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 | 0016829 | molecular_function | lyase 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 | 0016829 | molecular_function | lyase 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 | 0016829 | molecular_function | lyase activity |
| F | 0016831 | molecular_function | carboxy-lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD B 7001 |
| Chain | Residue |
| A | GLU109 |
| B | PHE34 |
| B | TYR77 |
| B | TYR79 |
| B | ILE81 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD F 7002 |
| Chain | Residue |
| F | TYR79 |
| F | ILE81 |
| D | GLU109 |
| D | HOH6487 |
| F | LEU31 |
| F | TYR77 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD D 7003 |
| Chain | Residue |
| D | LEU31 |
| D | PHE34 |
| D | TYR79 |
| D | ILE81 |
| E | GLU109 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MRD E 7004 |
| Chain | Residue |
| E | LEU31 |
| E | TYR77 |
| E | TYR79 |
| E | ILE81 |
| F | GLU109 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD C 7005 |
| Chain | Residue |
| B | GLU109 |
| C | LEU31 |
| C | PHE34 |
| C | TYR77 |
| C | TYR79 |
| C | ILE81 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MRD A 7006 |
| Chain | Residue |
| A | TYR79 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MRD D 7007 |
| Chain | Residue |
| D | PHE131 |
| D | GLU132 |
| D | GLY135 |
| D | TRP136 |
| F | GLY135 |
| F | TRP136 |
| F | GLU137 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MRD B 7008 |
| Chain | Residue |
| B | GLU132 |
| B | GLY135 |
| B | TRP136 |
| C | GLY135 |
| C | TRP136 |
| C | GLU137 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Site: {"description":"Cleavage (non-hydrolytic)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Pyruvic acid (Ser)","evidences":[{"source":"PubMed","id":"11980912","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| A | ASN47 | |
| A | SER52 | |
| A | ALA53 | |
| A | GLU109 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| B | ASN47 | |
| B | SER52 | |
| B | ALA53 | |
| B | GLU109 | proton shuttle (general acid/base) |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| C | ASN47 | |
| C | SER52 | |
| C | ALA53 | |
| C | GLU109 | proton shuttle (general acid/base) |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| D | ASN47 | |
| D | SER52 | |
| D | ALA53 | |
| D | GLU109 | proton shuttle (general acid/base) |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| E | ASN47 | |
| E | SER52 | |
| E | ALA53 | |
| E | GLU109 | proton shuttle (general acid/base) |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 707 |
| Chain | Residue | Details |
| F | ASN47 | |
| F | SER52 | |
| F | ALA53 | |
| F | GLU109 | proton shuttle (general acid/base) |
