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 | 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 | 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 | 18 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01939","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15723538","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01939","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12706720","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15723538","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 | HIS113 | |
| A | CYS123 | |
| A | ARG158 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1f8m |
| Chain | Residue | Details |
| B | HIS113 | |
| B | CYS123 | |
| B | ARG158 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 182 |
| Chain | Residue | Details |
| A | TYR43 | proton acceptor, proton donor |
| A | ASN210 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP58 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP85 | metal ligand |
| A | ASP87 | metal ligand |
| A | HIS113 | proton acceptor, proton donor, proton relay |
| A | GLU115 | proton acceptor, proton donor, proton relay |
| A | CYS123 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG158 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 182 |
| Chain | Residue | Details |
| B | TYR43 | proton acceptor, proton donor |
| B | ASN210 | electrostatic stabiliser, hydrogen bond donor |
| B | ASP58 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP85 | metal ligand |
| B | ASP87 | metal ligand |
| B | HIS113 | proton acceptor, proton donor, proton relay |
| B | GLU115 | proton acceptor, proton donor, proton relay |
| B | CYS123 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG158 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU188 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
