2VWT
Crystal structure of YfaU, a metal ion dependent class II aldolase from Escherichia coli K12 - Mg-pyruvate product complex
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 | 6 |
Details | BINDING SITE FOR RESIDUE MG A 301 |
Chain | Residue |
A | GLN151 |
A | GLU153 |
A | ASP179 |
A | PYR302 |
A | HOH2040 |
A | HOH2154 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PYR A 302 |
Chain | Residue |
A | PHE174 |
A | GLY176 |
A | PRO177 |
A | ALA178 |
A | ASP179 |
A | LEU216 |
A | MG301 |
A | ARG74 |
A | GLN151 |
A | GLU153 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 301 |
Chain | Residue |
B | GLN151 |
B | GLU153 |
B | ASP179 |
B | PYR302 |
B | HOH2035 |
C | HOH2094 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PYR B 302 |
Chain | Residue |
B | ARG74 |
B | GLN151 |
B | GLU153 |
B | PHE174 |
B | GLY176 |
B | PRO177 |
B | ALA178 |
B | ASP179 |
B | MG301 |
C | HOH2094 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 301 |
Chain | Residue |
A | HOH2112 |
C | GLN151 |
C | GLU153 |
C | ASP179 |
C | PYR302 |
C | HOH2112 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PYR C 302 |
Chain | Residue |
C | ARG74 |
C | GLN151 |
C | GLU153 |
C | GLY176 |
C | PRO177 |
C | ALA178 |
C | ASP179 |
C | LEU216 |
C | MG301 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A1257 |
Chain | Residue |
A | THR27 |
A | ALA29 |
A | ASP56 |
A | HIS59 |
A | HOH2201 |
A | HOH2202 |
A | HOH2203 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B1257 |
Chain | Residue |
B | THR27 |
B | ALA29 |
B | ASP56 |
B | HIS59 |
B | HOH2178 |
B | HOH2179 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 C1257 |
Chain | Residue |
C | THR27 |
C | THR28 |
C | ALA29 |
C | ASP56 |
C | HIS59 |
C | HOH2157 |
C | HOH2158 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C1258 |
Chain | Residue |
C | GLY78 |
C | PRO97 |
C | MET98 |
C | GLN104 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | HIS49 | |
B | HIS49 | |
C | HIS49 |
site_id | SWS_FT_FI2 |
Number of Residues | 9 |
Details | BINDING: |
Chain | Residue | Details |
A | GLN151 | |
A | ALA178 | |
A | ASP179 | |
B | GLN151 | |
B | ALA178 | |
B | ASP179 | |
C | GLN151 | |
C | ALA178 | |
C | ASP179 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:18754683 |
Chain | Residue | Details |
A | GLU153 | |
B | GLU153 | |
C | GLU153 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ARG74 | |
B | ARG74 | |
C | ARG74 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | SITE: Increases basicity of active site His |
Chain | Residue | Details |
A | ASP88 | |
B | ASP88 | |
C | ASP88 |
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 |