1F61
CRYSTAL STRUCTURE OF ISOCITRATE LYASE FROM MYCOBACTERIUM TUBERCULOSIS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004451 | molecular_function | isocitrate lyase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006097 | biological_process | glyoxylate cycle |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0006102 | biological_process | isocitrate metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019752 | biological_process | carboxylic acid metabolic process |
A | 0035375 | molecular_function | zymogen binding |
A | 0046421 | molecular_function | methylisocitrate lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0052572 | biological_process | response to host immune response |
A | 0071456 | biological_process | cellular response to hypoxia |
B | 0003824 | molecular_function | catalytic activity |
B | 0004451 | molecular_function | isocitrate lyase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006097 | biological_process | glyoxylate cycle |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0006102 | biological_process | isocitrate metabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0019752 | biological_process | carboxylic acid metabolic process |
B | 0035375 | molecular_function | zymogen binding |
B | 0046421 | molecular_function | methylisocitrate lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0052572 | biological_process | response to host immune response |
B | 0071456 | biological_process | cellular response to hypoxia |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 451 |
Chain | Residue |
A | ASP108 |
A | GLU155 |
A | HOH575 |
A | HOH690 |
A | HOH699 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 452 |
Chain | Residue |
B | HOH705 |
B | ASP108 |
B | GLU155 |
B | HOH595 |
B | HOH635 |
Functional Information from PROSITE/UniProt
site_id | PS00161 |
Number of Residues | 6 |
Details | ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHL |
Chain | Residue | Details |
A | LYS189-LEU194 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24354272 |
Chain | Residue | Details |
A | LYS190 | |
B | LYS190 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10932251 |
Chain | Residue | Details |
A | LEU90 | |
B | ALA227 | |
B | TYR312 | |
B | ILE346 | |
A | ALA152 | |
A | CYS191 | |
A | ALA227 | |
A | TYR312 | |
A | ILE346 | |
B | LEU90 | |
B | ALA152 | |
B | CYS191 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) => ECO:0000269|PubMed:20066036 |
Chain | Residue | Details |
A | GLN333 | |
B | GLN333 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1f8m |
Chain | Residue | Details |
A | ARG228 | |
A | HIS180 | |
A | CYS191 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1f8m |
Chain | Residue | Details |
B | ARG228 | |
B | HIS180 | |
B | CYS191 |
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
A | ALA152 | metal ligand |
A | SER179 | electrostatic stabiliser, hydrogen bond donor |
A | LYS190 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
A | GLY192 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
A | ALA227 | electrostatic stabiliser, hydrogen bond donor |
A | CYS314 | electrostatic stabiliser, hydrogen bond donor |
A | PRO316 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
B | ALA152 | metal ligand |
B | SER179 | electrostatic stabiliser, hydrogen bond donor |
B | LYS190 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
B | GLY192 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
B | ALA227 | electrostatic stabiliser, hydrogen bond donor |
B | CYS314 | electrostatic stabiliser, hydrogen bond donor |
B | PRO316 | electrostatic stabiliser, hydrogen bond donor |