2IXJ
RmlC P aeruginosa native
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0005829 | cellular_component | cytosol |
| A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| A | 0009103 | biological_process | lipopolysaccharide biosynthetic process |
| A | 0009244 | biological_process | lipopolysaccharide core region biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SRT A1185 |
| Chain | Residue |
| A | ARG62 |
| A | HOH2067 |
| A | HOH2085 |
| A | HOH2086 |
| A | HOH2087 |
| A | HIS65 |
| A | LYS74 |
| A | ARG92 |
| A | HIS121 |
| A | TYR134 |
| A | TRP140 |
| A | GLU145 |
| A | HOH2029 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IXI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2003","submissionDatabase":"PDB data bank","title":"RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure.","authors":["Dong C.J.","Naismith J.H."]}},{"source":"PDB","id":"1RTV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IXH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose","evidences":[{"source":"UniProtKB","id":"Q5SFD1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dzr |
| Chain | Residue | Details |
| A | HIS65 | |
| A | ASP171 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 329 |
| Chain | Residue | Details |
| A | HIS65 | proton acceptor, proton donor |
| A | LYS74 | electrostatic stabiliser |
| A | TYR134 | proton acceptor, proton donor, proton relay |
| A | ASP171 | electrostatic stabiliser, increase acidity, increase basicity |
