2VWS
Crystal structure of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016151 | molecular_function | nickel cation binding |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016832 | molecular_function | aldehyde-lyase activity |
| A | 0034214 | biological_process | protein hexamerization |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| A | 0106099 | molecular_function | 2-keto-3-deoxy-L-rhamnonate aldolase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016151 | molecular_function | nickel cation binding |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016832 | molecular_function | aldehyde-lyase activity |
| B | 0034214 | biological_process | protein hexamerization |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| B | 0106099 | molecular_function | 2-keto-3-deoxy-L-rhamnonate aldolase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016151 | molecular_function | nickel cation binding |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016832 | molecular_function | aldehyde-lyase activity |
| C | 0034214 | biological_process | protein hexamerization |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0061677 | molecular_function | 2-dehydro-3-deoxy-D-gluconate aldolase activity |
| C | 0106099 | molecular_function | 2-keto-3-deoxy-L-rhamnonate aldolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A1257 |
| Chain | Residue |
| A | THR27 |
| A | THR28 |
| A | ALA29 |
| A | ASP56 |
| A | HIS59 |
| A | HOH2316 |
| A | HOH2317 |
| A | HOH2319 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B1257 |
| Chain | Residue |
| B | THR28 |
| B | ALA29 |
| B | ASP56 |
| B | HIS59 |
| B | HOH2320 |
| B | HOH2321 |
| B | THR27 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A1258 |
| Chain | Residue |
| A | LEU5 |
| A | SER6 |
| A | GLN92 |
| A | HOH2005 |
| A | HOH2193 |
| A | HOH2320 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 C1257 |
| Chain | Residue |
| C | THR27 |
| C | THR28 |
| C | ALA29 |
| C | ASP56 |
| C | HIS59 |
| C | HOH2313 |
| C | HOH2315 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL C1258 |
| Chain | Residue |
| C | GLY78 |
| C | SER79 |
| C | PRO97 |
| C | MET98 |
| C | GLN104 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C1259 |
| Chain | Residue |
| A | VAL122 |
| C | ARG74 |
| C | GLN151 |
| C | ASP179 |
| C | HOH2316 |
| C | HOH2317 |
| C | HOH2318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18754683","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Site: {"description":"Increases basicity of active site His"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dxe |
| Chain | Residue | Details |
| A | HIS49 | |
| A | ARG74 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dxe |
| Chain | Residue | Details |
| B | HIS49 | |
| B | ARG74 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dxe |
| Chain | Residue | Details |
| C | HIS49 | |
| C | ARG74 |
