Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0019571 | biological_process | D-arabinose catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| X | 0000287 | molecular_function | magnesium ion binding |
| X | 0003824 | molecular_function | catalytic activity |
| X | 0016829 | molecular_function | lyase activity |
| X | 0016836 | molecular_function | hydro-lyase activity |
| X | 0019571 | biological_process | D-arabinose catabolic process |
| X | 0046872 | molecular_function | metal ion binding |
| X | 0051289 | biological_process | protein homotetramerization |
| Y | 0000287 | molecular_function | magnesium ion binding |
| Y | 0003824 | molecular_function | catalytic activity |
| Y | 0016829 | molecular_function | lyase activity |
| Y | 0016836 | molecular_function | hydro-lyase activity |
| Y | 0019571 | biological_process | D-arabinose catabolic process |
| Y | 0046872 | molecular_function | metal ion binding |
| Y | 0051289 | biological_process | protein homotetramerization |
| Z | 0000287 | molecular_function | magnesium ion binding |
| Z | 0003824 | molecular_function | catalytic activity |
| Z | 0016829 | molecular_function | lyase activity |
| Z | 0016836 | molecular_function | hydro-lyase activity |
| Z | 0019571 | biological_process | D-arabinose catabolic process |
| Z | 0046872 | molecular_function | metal ion binding |
| Z | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG Y 294 |
| Chain | Residue |
| Y | GLU143 |
| Y | GLU145 |
| Y | ASP164 |
| Y | LYS182 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG Z 294 |
| Chain | Residue |
| Z | GLU143 |
| Z | GLU145 |
| Z | ASP164 |
| Z | LYS182 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG X 294 |
| Chain | Residue |
| X | GLU145 |
| X | ASP164 |
| X | LYS182 |
| X | GLU143 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 294 |
| Chain | Residue |
| A | GLU143 |
| A | GLU145 |
| A | ASP164 |
| A | LYS182 |
Functional Information from PROSITE/UniProt
| site_id | PS00307 |
| Number of Residues | 7 |
| Details | LECTIN_LEGUME_BETA Legume lectins beta-chain signature. LAVVLDS |
| Chain | Residue | Details |
| A | LEU146-SER152 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| Z | ILE81 | |
| Z | GLU143 | |
| Z | GLU145 | |
| Z | ASP164 | |
| Z | LYS182 | |
| Z | THR256 | |
| Y | ILE81 | |
| Y | GLU143 | |
| Y | GLU145 | |
| Y | ASP164 | |
| Y | LYS182 | |
| Y | THR256 | |
| A | ILE81 | |
| A | GLU143 | |
| A | GLU145 | |
| A | ASP164 | |
| A | LYS182 | |
| A | THR256 | |
| X | ILE81 | |
| X | GLU143 | |
| X | GLU145 | |
| X | ASP164 | |
| X | LYS182 | |
| X | THR256 | |
