Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0015977 | biological_process | carbon fixation |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0015977 | biological_process | carbon fixation |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | binding site for residue CAP A 501 |
| Chain | Residue |
| A | THR177 |
| A | LYS338 |
| A | LEU339 |
| A | SER383 |
| A | GLY384 |
| A | GLY385 |
| A | GLY407 |
| A | GLY408 |
| A | MG502 |
| A | HOH606 |
| A | HOH624 |
| A | LYS179 |
| A | HOH659 |
| A | HOH673 |
| A | HOH688 |
| A | HOH694 |
| B | GLU71 |
| B | THR76 |
| B | TRP77 |
| B | ASN127 |
| B | HOH686 |
| A | LYS181 |
| A | KCX205 |
| A | ASP207 |
| A | GLU208 |
| A | HIS298 |
| A | ARG299 |
| A | HIS331 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | LYS181 |
| A | KCX205 |
| A | ASP207 |
| A | GLU208 |
| A | CAP501 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue CAP B 501 |
| Chain | Residue |
| A | GLU71 |
| A | THR76 |
| A | TRP77 |
| A | ASN127 |
| A | HOH625 |
| A | HOH656 |
| B | THR177 |
| B | LYS179 |
| B | LYS181 |
| B | KCX205 |
| B | ASP207 |
| B | GLU208 |
| B | HIS298 |
| B | ARG299 |
| B | HIS331 |
| B | LYS338 |
| B | LEU339 |
| B | SER383 |
| B | GLY384 |
| B | GLY385 |
| B | GLY407 |
| B | GLY408 |
| B | MG502 |
| B | HOH627 |
| B | HOH645 |
| B | HOH646 |
| B | HOH647 |
| B | HOH653 |
| B | HOH675 |
| B | HOH731 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | KCX205 |
| B | ASP207 |
| B | GLU208 |
| B | CAP501 |
| site_id | AC5 |
| Number of Residues | 28 |
| Details | binding site for residue CAP C 501 |
| Chain | Residue |
| C | THR177 |
| C | LYS179 |
| C | LYS181 |
| C | KCX205 |
| C | ASP207 |
| C | GLU208 |
| C | HIS298 |
| C | ARG299 |
| C | HIS331 |
| C | LYS338 |
| C | LEU339 |
| C | SER383 |
| C | GLY384 |
| C | GLY385 |
| C | GLY407 |
| C | GLY408 |
| C | MG502 |
| C | HOH610 |
| C | HOH612 |
| C | HOH651 |
| C | HOH655 |
| C | HOH663 |
| C | HOH696 |
| C | HOH768 |
| D | GLU71 |
| D | THR76 |
| D | TRP77 |
| D | ASN127 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | GLU208 |
| C | CAP501 |
| C | LYS179 |
| C | LYS181 |
| C | KCX205 |
| C | ASP207 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | binding site for residue CAP D 501 |
| Chain | Residue |
| C | THR76 |
| C | TRP77 |
| C | ASN127 |
| C | HOH636 |
| D | THR177 |
| D | LYS179 |
| D | LYS181 |
| D | KCX205 |
| D | ASP207 |
| D | GLU208 |
| D | HIS298 |
| D | ARG299 |
| D | HIS331 |
| D | LYS338 |
| D | LEU339 |
| D | SER383 |
| D | GLY384 |
| D | GLY385 |
| D | GLY407 |
| D | GLY408 |
| D | MG502 |
| D | HOH621 |
| D | HOH626 |
| D | HOH628 |
| D | HOH631 |
| D | HOH642 |
| D | HOH663 |
| D | HOH683 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| C | ASN127 |
| D | LYS181 |
| D | KCX205 |
| D | ASP207 |
| D | GLU208 |
| D | CAP501 |
Functional Information from PROSITE/UniProt
| site_id | PS00213 |
| Number of Residues | 12 |
| Details | LIPOCALIN Lipocalin signature. ETN..EFKGHWHNV |
| Chain | Residue | Details |
| A | GLU235-VAL246 | |
