Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000271 | biological_process | polysaccharide biosynthetic process |
A | 0008483 | molecular_function | transaminase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0017000 | biological_process | antibiotic biosynthetic process |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PLP A 389 |
Chain | Residue |
A | ASN61 |
A | LYS188 |
A | ASN234 |
A | HOH392 |
A | HOH461 |
A | HOH561 |
A | HOH567 |
A | GLY62 |
A | THR63 |
A | THR87 |
A | ASP159 |
A | ALA161 |
A | HIS162 |
A | SER183 |
A | GLN185 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
Chain | Residue | Details |
A | LYS188 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | a catalytic site defined by CSA, PubMed 10433690 |
Chain | Residue | Details |
A | PHE88 | |
A | LYS188 | |
A | ASP159 | |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 419 |
Chain | Residue | Details |
A | PHE88 | electrostatic stabiliser |
A | ASP159 | electrostatic stabiliser |
A | HIS162 | steric role |
A | GLN185 | proton shuttle (general acid/base) |
A | LYS188 | covalent catalysis, proton shuttle (general acid/base) |
A | ARG219 | steric role |
A | TYR226 | steric role |
A | ARG236 | steric role |