1F8I
CRYSTAL STRUCTURE OF ISOCITRATE LYASE:NITROPROPIONATE:GLYOXYLATE COMPLEX 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 |
C | 0003824 | molecular_function | catalytic activity |
C | 0004451 | molecular_function | isocitrate lyase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006097 | biological_process | glyoxylate cycle |
C | 0006099 | biological_process | tricarboxylic acid cycle |
C | 0006102 | biological_process | isocitrate metabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0019752 | biological_process | carboxylic acid metabolic process |
C | 0035375 | molecular_function | zymogen binding |
C | 0046421 | molecular_function | methylisocitrate lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0052572 | biological_process | response to host immune response |
C | 0071456 | biological_process | cellular response to hypoxia |
D | 0003824 | molecular_function | catalytic activity |
D | 0004451 | molecular_function | isocitrate lyase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0005829 | cellular_component | cytosol |
D | 0005886 | cellular_component | plasma membrane |
D | 0006097 | biological_process | glyoxylate cycle |
D | 0006099 | biological_process | tricarboxylic acid cycle |
D | 0006102 | biological_process | isocitrate metabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0019752 | biological_process | carboxylic acid metabolic process |
D | 0035375 | molecular_function | zymogen binding |
D | 0046421 | molecular_function | methylisocitrate lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0052572 | biological_process | response to host immune response |
D | 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 | ASP153 |
A | GLV461 |
A | HOH1001 |
A | HOH1002 |
A | HOH1003 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 452 |
Chain | Residue |
B | HOH1005 |
B | HOH1006 |
B | ASP108 |
B | ASP153 |
B | GLV462 |
B | HOH1004 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG C 453 |
Chain | Residue |
C | ASP153 |
C | GLV463 |
C | HOH1007 |
C | HOH1008 |
C | HOH1009 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 454 |
Chain | Residue |
D | ASP153 |
D | GLV464 |
D | HOH1010 |
D | HOH1011 |
D | HOH1012 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GLV A 461 |
Chain | Residue |
A | TYR89 |
A | SER91 |
A | GLY92 |
A | TRP93 |
A | ASP153 |
A | ARG228 |
A | TRP283 |
A | THR347 |
A | MG451 |
A | SIN471 |
A | HOH1002 |
site_id | AC6 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLV B 462 |
Chain | Residue |
B | TYR89 |
B | SER91 |
B | GLY92 |
B | TRP93 |
B | ASP153 |
B | ARG228 |
B | TRP283 |
B | THR347 |
B | MG452 |
B | SIN472 |
B | HOH1004 |
B | HOH1005 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE GLV C 463 |
Chain | Residue |
C | TYR89 |
C | SER91 |
C | GLY92 |
C | TRP93 |
C | ASP153 |
C | ARG228 |
C | TRP283 |
C | THR347 |
C | MG453 |
C | SIN473 |
C | HOH1009 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE GLV D 464 |
Chain | Residue |
D | TYR89 |
D | SER91 |
D | GLY92 |
D | TRP93 |
D | ASP153 |
D | ARG228 |
D | THR347 |
D | MG454 |
D | SIN474 |
D | HOH1010 |
D | HOH1011 |
D | HOH1012 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SIN A 471 |
Chain | Residue |
A | SER191 |
A | GLY192 |
A | HIS193 |
A | ARG228 |
A | GLU285 |
A | ASN313 |
A | SER315 |
A | SER317 |
A | THR347 |
A | GLV461 |
A | HOH1002 |
A | HOH1679 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE SIN B 472 |
Chain | Residue |
B | ASP108 |
B | SER191 |
B | GLY192 |
B | HIS193 |
B | ARG228 |
B | GLU285 |
B | ASN313 |
B | SER315 |
B | SER317 |
B | THR347 |
B | GLV462 |
B | HOH1005 |
B | HOH1680 |
site_id | BC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE SIN C 473 |
Chain | Residue |
C | SER317 |
C | THR347 |
C | GLV463 |
C | HOH1008 |
C | HOH1681 |
C | SER191 |
C | GLY192 |
C | HIS193 |
C | ARG228 |
C | GLU285 |
C | ASN313 |
C | SER315 |
site_id | BC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE SIN D 474 |
Chain | Residue |
D | ASP108 |
D | SER191 |
D | GLY192 |
D | HIS193 |
D | ARG228 |
D | GLU285 |
D | ASN313 |
D | SER315 |
D | SER317 |
D | THR347 |
D | GLV464 |
D | HOH1011 |
D | HOH1682 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24354272 |
Chain | Residue | Details |
A | LYS190 | |
B | LYS190 | |
C | LYS190 | |
D | LYS190 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10932251 |
Chain | Residue | Details |
A | LEU90 | |
B | ALA227 | |
B | TYR312 | |
B | ILE346 | |
C | LEU90 | |
C | ALA152 | |
C | SER191 | |
C | ALA227 | |
C | TYR312 | |
C | ILE346 | |
D | LEU90 | |
A | ALA152 | |
D | ALA152 | |
D | SER191 | |
D | ALA227 | |
D | TYR312 | |
D | ILE346 | |
A | SER191 | |
A | ALA227 | |
A | TYR312 | |
A | ILE346 | |
B | LEU90 | |
B | ALA152 | |
B | SER191 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
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 | |
C | GLN333 | |
D | 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 | SER191 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1f8m |
Chain | Residue | Details |
B | ARG228 | |
B | HIS180 | |
B | SER191 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1f8m |
Chain | Residue | Details |
C | ARG228 | |
C | HIS180 | |
C | SER191 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1f8m |
Chain | Residue | Details |
D | ARG228 | |
D | HIS180 | |
D | SER191 |
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 |
site_id | MCSA3 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
C | ALA152 | metal ligand |
C | SER179 | electrostatic stabiliser, hydrogen bond donor |
C | LYS190 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
C | GLY192 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
C | ALA227 | electrostatic stabiliser, hydrogen bond donor |
C | CYS314 | electrostatic stabiliser, hydrogen bond donor |
C | PRO316 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 7 |
Details | M-CSA 272 |
Chain | Residue | Details |
D | ALA152 | metal ligand |
D | SER179 | electrostatic stabiliser, hydrogen bond donor |
D | LYS190 | covalent catalysis, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, proton shuttle (general acid/base) |
D | GLY192 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton shuttle (general acid/base) |
D | ALA227 | electrostatic stabiliser, hydrogen bond donor |
D | CYS314 | electrostatic stabiliser, hydrogen bond donor |
D | PRO316 | electrostatic stabiliser, hydrogen bond donor |