1MUM
Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 1001 |
Chain | Residue |
A | ASP58 |
A | ASP87 |
A | HOH1006 |
A | HOH1031 |
A | HOH1044 |
A | HOH1076 |
A | HOH1093 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1002 |
Chain | Residue |
B | HOH1047 |
B | HOH1058 |
B | HOH1125 |
B | HOH1173 |
B | ASP58 |
B | ASP87 |
Functional Information from PROSITE/UniProt
site_id | PS00161 |
Number of Residues | 6 |
Details | ISOCITRATE_LYASE Isocitrate lyase signature. KRCGHR |
Chain | Residue | Details |
A | LYS121-ARG126 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:15723538 |
Chain | Residue | Details |
A | GLY46 | |
B | THR159 | |
B | ALA189 | |
B | ILE211 | |
B | ALA242 | |
B | ASN271 | |
A | GLY124 | |
A | THR159 | |
A | ALA189 | |
A | ILE211 | |
A | ALA242 | |
A | ASN271 | |
B | GLY46 | |
B | GLY124 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:12706720, ECO:0000269|PubMed:15723538 |
Chain | Residue | Details |
A | ALA86 | |
A | ILE88 | |
B | ALA86 | |
B | ILE88 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 182 |
Chain | Residue | Details |
A | LEU44 | proton acceptor, proton donor |
A | ILE211 | electrostatic stabiliser, hydrogen bond donor |
A | LEU59 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ALA86 | metal ligand |
A | ILE88 | metal ligand |
A | ILE114 | proton acceptor, proton donor, proton relay |
A | ASP116 | proton acceptor, proton donor, proton relay |
A | GLY124 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | THR159 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | ALA189 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 182 |
Chain | Residue | Details |
B | LEU44 | proton acceptor, proton donor |
B | ILE211 | electrostatic stabiliser, hydrogen bond donor |
B | LEU59 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ALA86 | metal ligand |
B | ILE88 | metal ligand |
B | ILE114 | proton acceptor, proton donor, proton relay |
B | ASP116 | proton acceptor, proton donor, proton relay |
B | GLY124 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | THR159 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
B | ALA189 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |