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 | 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 | 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"24354272","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10932251","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)","evidences":[{"source":"PubMed","id":"20066036","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | ASP153 | metal ligand |
| A | HIS180 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
| A | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
| A | ARG228 | electrostatic stabiliser, hydrogen bond donor |
| A | SER315 | electrostatic stabiliser, hydrogen bond donor |
| A | SER317 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 272 |
| Chain | Residue | Details |
| B | ASP153 | metal ligand |
| B | HIS180 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS191 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
| B | HIS193 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
| B | ARG228 | electrostatic stabiliser, hydrogen bond donor |
| B | SER315 | electrostatic stabiliser, hydrogen bond donor |
| B | SER317 | electrostatic stabiliser, hydrogen bond donor |
