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 | 0016833 | molecular_function | oxo-acid-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 | 0016833 | molecular_function | oxo-acid-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 | 0016833 | molecular_function | oxo-acid-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 | 0016833 | molecular_function | oxo-acid-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 |