2I5Q
Crystal structure of Apo L-rhamnonate dehydratase from Escherichia Coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0009063 | biological_process | amino acid catabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009063 | biological_process | amino acid catabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050032 | molecular_function | L-rhamnonate dehydratase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00908 |
| Number of Residues | 26 |
| Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. TiSCVDlALwDLfGKvvglPVykLLG |
| Chain | Residue | Details |
| A | THR136-GLY161 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01288 |
| Chain | Residue | Details |
| A | LEU325 | |
| B | LEU325 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01288 |
| Chain | Residue | Details |
| A | GLY29 | |
| B | LEU248 | |
| B | VAL276 | |
| B | THR345 | |
| A | TYR55 | |
| A | TRP222 | |
| A | LEU248 | |
| A | VAL276 | |
| A | THR345 | |
| B | GLY29 | |
| B | TYR55 | |
| B | TRP222 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Increases basicity of active site His => ECO:0000255|HAMAP-Rule:MF_01288 |
| Chain | Residue | Details |
| A | ILE298 | |
| B | ILE298 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01288 |
| Chain | Residue | Details |
| A | THR345 | |
| B | THR345 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS329 | |
| B | HIS329 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | HIS33 | |
| B | HIS33 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG59 | |
| B | GLU349 | |
| A | ASP226 | |
| A | GLU252 | |
| A | GLU280 | |
| A | GLU349 | |
| B | ARG59 | |
| B | ASP226 | |
| B | GLU252 | |
| B | GLU280 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Increases basicity of active site His => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP302 | |
| B | ASP302 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU349 | |
| B | GLU349 |
