2UYU
L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A88F- E192A)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005996 | biological_process | monosaccharide metabolic process |
A | 0008994 | molecular_function | rhamnulose-1-phosphate aldolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016830 | molecular_function | carbon-carbon lyase activity |
A | 0016832 | molecular_function | aldehyde-lyase activity |
A | 0019299 | biological_process | rhamnose metabolic process |
A | 0019301 | biological_process | rhamnose catabolic process |
A | 0019323 | biological_process | pentose catabolic process |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0005996 | biological_process | monosaccharide metabolic process |
E | 0008994 | molecular_function | rhamnulose-1-phosphate aldolase activity |
E | 0016829 | molecular_function | lyase activity |
E | 0016830 | molecular_function | carbon-carbon lyase activity |
E | 0016832 | molecular_function | aldehyde-lyase activity |
E | 0019299 | biological_process | rhamnose metabolic process |
E | 0019301 | biological_process | rhamnose catabolic process |
E | 0019323 | biological_process | pentose catabolic process |
E | 0042802 | molecular_function | identical protein binding |
E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A1275 |
Chain | Residue |
A | HIS141 |
A | HIS143 |
A | GLU171 |
A | HIS212 |
A | HOH2167 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE A1276 |
Chain | Residue |
E | GLU254 |
E | HOH2161 |
A | HIS204 |
A | HOH2123 |
A | HOH2125 |
A | HOH2126 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E1275 |
Chain | Residue |
E | HIS141 |
E | HIS143 |
E | GLU171 |
E | HIS212 |
E | HOH2174 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE FE E1276 |
Chain | Residue |
E | HIS204 |
E | HOH2122 |
E | HOH2123 |
E | HOH2124 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479 |
Chain | Residue | Details |
A | GLU117 | |
E | GLU117 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11976494, ECO:0000269|PubMed:12962479 |
Chain | Residue | Details |
A | HIS141 | |
A | HIS143 | |
A | HIS212 | |
E | HIS141 | |
E | HIS143 | |
E | HIS212 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 645 |
Chain | Residue | Details |
A | GLU117 | proton acceptor, proton donor |
A | HIS141 | metal ligand |
A | HIS143 | metal ligand |
A | GLU171 | proton donor |
A | HIS212 | metal ligand |
site_id | MCSA2 |
Number of Residues | 5 |
Details | M-CSA 645 |
Chain | Residue | Details |
E | GLU117 | proton acceptor, proton donor |
E | HIS141 | metal ligand |
E | HIS143 | metal ligand |
E | GLU171 | proton donor |
E | HIS212 | metal ligand |