6T5M
Crystal structure of 2-methylisocitrate lyase (PrpB) from Pseudomonas aeruginosa in complex with Mg(II)-pyruvate.
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 | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| A | 0046421 | molecular_function | methylisocitrate lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| B | 0046421 | molecular_function | methylisocitrate lyase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| C | 0046421 | molecular_function | methylisocitrate lyase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019629 | biological_process | propionate catabolic process, 2-methylcitrate cycle |
| D | 0046421 | molecular_function | methylisocitrate lyase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 301 |
| Chain | Residue |
| C | ASP87 |
| C | PYR302 |
| C | HOH422 |
| C | HOH448 |
| C | HOH502 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue PYR C 302 |
| Chain | Residue |
| C | ASP87 |
| C | ARG160 |
| C | MG301 |
| C | HOH412 |
| C | HOH448 |
| C | TYR45 |
| C | SER47 |
| C | GLY48 |
| C | GLY49 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 301 |
| Chain | Residue |
| A | ASP87 |
| A | PYR302 |
| A | HOH405 |
| A | HOH414 |
| A | HOH493 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PYR A 302 |
| Chain | Residue |
| A | TYR45 |
| A | SER47 |
| A | GLY48 |
| A | GLY49 |
| A | ASP87 |
| A | ARG160 |
| A | MG301 |
| A | HOH493 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 301 |
| Chain | Residue |
| D | ASP87 |
| D | PYR302 |
| D | HOH413 |
| D | HOH437 |
| D | HOH472 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue PYR D 302 |
| Chain | Residue |
| D | TYR45 |
| D | SER47 |
| D | GLY48 |
| D | GLY49 |
| D | ASP87 |
| D | ARG160 |
| D | PRO238 |
| D | MG301 |
| D | HOH413 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 301 |
| Chain | Residue |
| B | ASP87 |
| B | PYR302 |
| B | HOH412 |
| B | HOH432 |
| B | HOH451 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue PYR B 302 |
| Chain | Residue |
| B | TYR45 |
| B | SER47 |
| B | GLY48 |
| B | GLY49 |
| B | ASP87 |
| B | ARG160 |
| B | PRO238 |
| B | MG301 |
| B | HOH451 |
Functional Information from PROSITE/UniProt
| site_id | PS00161 |
| Number of Residues | 6 |
| Details | ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR |
| Chain | Residue | Details |
| C | LYS123-ARG128 |
