1PM7
RmlC (dTDP-6-DEOXY-D-XYLO-4-HEXULOSE 3,5-EPIMERASE)STRUCTURE FROM MYCOBACTERIUM TUBERCULOSIS AND INHIBITOR DESIGN. THE APO STRUCTURE.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000271 | biological_process | polysaccharide biosynthetic process |
| A | 0005515 | molecular_function | protein binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
| B | 0000271 | biological_process | polysaccharide biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0008830 | molecular_function | dTDP-4-dehydrorhamnose 3,5-epimerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019305 | biological_process | dTDP-rhamnose biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 260 |
| Chain | Residue |
| A | HIS62 |
| A | LYS72 |
| A | HIS119 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 261 |
| Chain | Residue |
| B | HIS62 |
| B | LYS72 |
| B | HIS119 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 250 |
| Chain | Residue |
| A | THR17 |
| A | MET1 |
| A | LYS2 |
| A | PRO16 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 251 |
| Chain | Residue |
| B | MET1 |
| B | PRO16 |
| B | GLU28 |
| B | TRP29 |
| B | LEU30 |
| B | GLY34 |
| B | PHE35 |
| B | TYR73 |
| B | HOH265 |
| B | HOH309 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IXC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q9HU21","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2IXC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2IXC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17046787","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12951098","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PM7","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":"PubMed","id":"12951098","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PM7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IXC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9HU21","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| 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 | HIS62 | |
| A | ASP171 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dzr |
| Chain | Residue | Details |
| B | HIS62 | |
| B | ASP171 |
