Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009058 | biological_process | biosynthetic process |
A | 0009236 | biological_process | cobalamin biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0048472 | molecular_function | threonine-phosphate decarboxylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 A 700 |
Chain | Residue |
A | HIS8 |
A | GLY9 |
A | ASN157 |
A | ARG323 |
A | TYR328 |
A | ARG337 |
A | HOH858 |
A | HOH917 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PLP A 800 |
Chain | Residue |
A | GLY84 |
A | GLU85 |
A | THR86 |
A | PHE108 |
A | CYS153 |
A | ASN157 |
A | ASP185 |
A | ALA187 |
A | PHE188 |
A | SER213 |
A | THR215 |
A | LYS216 |
A | ARG224 |
A | TYR56 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 701 |
Chain | Residue |
A | ASP190 |
A | ARG212 |
A | SER213 |
A | TYR227 |
A | HOH820 |
A | HOH822 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 702 |
Chain | Residue |
A | LEU152 |
A | CYS153 |
A | ASN156 |
A | PRO163 |
A | HOH809 |
A | HOH1201 |
Functional Information from PROSITE/UniProt
site_id | PS00105 |
Number of Residues | 14 |
Details | AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLTKfyAIpGLRLG |
Chain | Residue | Details |
A | SER213-GLY226 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS8 | |
A | ASN32 | |
A | ASN157 | |
A | ARG323 | |
A | ARG337 | |
Chain | Residue | Details |
A | LYS216 | |