1DE6
L-RHAMNOSE ISOMERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008740 | molecular_function | L-rhamnose isomerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019301 | biological_process | rhamnose catabolic process |
| A | 0019318 | biological_process | hexose metabolic process |
| A | 0019324 | biological_process | L-lyxose metabolic process |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0033296 | molecular_function | rhamnose binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008740 | molecular_function | L-rhamnose isomerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019301 | biological_process | rhamnose catabolic process |
| B | 0019318 | biological_process | hexose metabolic process |
| B | 0019324 | biological_process | L-lyxose metabolic process |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0033296 | molecular_function | rhamnose binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0008740 | molecular_function | L-rhamnose isomerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019301 | biological_process | rhamnose catabolic process |
| C | 0019318 | biological_process | hexose metabolic process |
| C | 0019324 | biological_process | L-lyxose metabolic process |
| C | 0030145 | molecular_function | manganese ion binding |
| C | 0032991 | cellular_component | protein-containing complex |
| C | 0033296 | molecular_function | rhamnose binding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0008740 | molecular_function | L-rhamnose isomerase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019301 | biological_process | rhamnose catabolic process |
| D | 0019318 | biological_process | hexose metabolic process |
| D | 0019324 | biological_process | L-lyxose metabolic process |
| D | 0030145 | molecular_function | manganese ion binding |
| D | 0032991 | cellular_component | protein-containing complex |
| D | 0033296 | molecular_function | rhamnose binding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RNS A 1462 |
| Chain | Residue |
| A | ILE67 |
| A | ZN450 |
| A | MN451 |
| A | HIS103 |
| A | TRP193 |
| A | GLU234 |
| A | LYS236 |
| A | HIS270 |
| A | ASP302 |
| A | ASP334 |
| A | PHE336 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RNS B 2462 |
| Chain | Residue |
| B | ILE67 |
| B | HIS103 |
| B | TRP193 |
| B | GLU234 |
| B | LYS236 |
| B | ASP267 |
| B | HIS270 |
| B | ASP302 |
| B | ASP334 |
| B | PHE336 |
| B | ZN450 |
| B | MN451 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE RNS C 3462 |
| Chain | Residue |
| C | ILE67 |
| C | HIS103 |
| C | TRP193 |
| C | GLU234 |
| C | LYS236 |
| C | HIS270 |
| C | ASP302 |
| C | ASP334 |
| C | PHE336 |
| C | ZN450 |
| C | MN451 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RNS D 4462 |
| Chain | Residue |
| D | ILE67 |
| D | HIS103 |
| D | TRP193 |
| D | GLU234 |
| D | LYS236 |
| D | ASP267 |
| D | HIS270 |
| D | ASP302 |
| D | ASP334 |
| D | PHE336 |
| D | ZN450 |
| D | MN451 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 450 |
| Chain | Residue |
| A | GLU234 |
| A | ASP267 |
| A | HIS294 |
| A | ASP334 |
| A | RNS1462 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN A 451 |
| Chain | Residue |
| A | HIS270 |
| A | ASP302 |
| A | ASP304 |
| A | RNS1462 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 450 |
| Chain | Residue |
| B | GLU234 |
| B | ASP267 |
| B | HIS294 |
| B | ASP334 |
| B | RNS2462 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN B 451 |
| Chain | Residue |
| B | HIS270 |
| B | ASP302 |
| B | ASP304 |
| B | RNS2462 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 450 |
| Chain | Residue |
| C | GLU234 |
| C | ASP267 |
| C | HIS294 |
| C | ASP334 |
| C | RNS3462 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN C 451 |
| Chain | Residue |
| C | HIS270 |
| C | ASP302 |
| C | ASP304 |
| C | RNS3462 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 450 |
| Chain | Residue |
| D | GLU234 |
| D | ASP267 |
| D | HIS294 |
| D | ASP334 |
| D | RNS4462 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 451 |
| Chain | Residue |
| D | HIS270 |
| D | ASP302 |
| D | ASP304 |
| D | RNS4462 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10891278","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DE6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10891278","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1D8W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DE5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DE6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00541","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10891278","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DE6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10891278 |
| Chain | Residue | Details |
| A | ASP302 | |
| A | LYS236 | |
| A | HIS270 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10891278 |
| Chain | Residue | Details |
| B | ASP302 | |
| B | LYS236 | |
| B | HIS270 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10891278 |
| Chain | Residue | Details |
| C | ASP302 | |
| C | LYS236 | |
| C | HIS270 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10891278 |
| Chain | Residue | Details |
| D | ASP302 | |
| D | LYS236 | |
| D | HIS270 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 488 |
| Chain | Residue | Details |
| A | TRP193 | activator |
| A | GLU234 | metal ligand |
| A | LYS236 | activator |
| A | ASP267 | metal ligand |
| A | HIS270 | activator, metal ligand |
| A | HIS294 | metal ligand |
| A | ASP302 | metal ligand |
| A | ASP304 | metal ligand, proton acceptor, proton donor |
| A | ASP334 | metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 488 |
| Chain | Residue | Details |
| B | TRP193 | activator |
| B | GLU234 | metal ligand |
| B | LYS236 | activator |
| B | ASP267 | metal ligand |
| B | HIS270 | activator, metal ligand |
| B | HIS294 | metal ligand |
| B | ASP302 | metal ligand |
| B | ASP304 | metal ligand, proton acceptor, proton donor |
| B | ASP334 | metal ligand, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 488 |
| Chain | Residue | Details |
| C | TRP193 | activator |
| C | GLU234 | metal ligand |
| C | LYS236 | activator |
| C | ASP267 | metal ligand |
| C | HIS270 | activator, metal ligand |
| C | HIS294 | metal ligand |
| C | ASP302 | metal ligand |
| C | ASP304 | metal ligand, proton acceptor, proton donor |
| C | ASP334 | metal ligand, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 488 |
| Chain | Residue | Details |
| D | TRP193 | activator |
| D | GLU234 | metal ligand |
| D | LYS236 | activator |
| D | ASP267 | metal ligand |
| D | HIS270 | activator, metal ligand |
| D | HIS294 | metal ligand |
| D | ASP302 | metal ligand |
| D | ASP304 | metal ligand, proton acceptor, proton donor |
| D | ASP334 | metal ligand, proton acceptor, proton donor |
