1RTV
RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| A | 0045226 | biological_process | extracellular polysaccharide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SRT A 182 |
| Chain | Residue |
| A | ARG59 |
| A | HIS62 |
| A | LYS71 |
| A | ARG89 |
| A | HIS118 |
| A | TYR131 |
| A | TRP137 |
| A | GLU142 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17046787 |
| Chain | Residue | Details |
| A | HIS62 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:17046787 |
| Chain | Residue | Details |
| A | TYR131 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXK |
| Chain | Residue | Details |
| A | ARG23 | |
| A | GLU28 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXH |
| Chain | Residue | Details |
| A | GLN47 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK |
| Chain | Residue | Details |
| A | ARG59 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK |
| Chain | Residue | Details |
| A | LYS71 | |
| A | HIS118 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXJ |
| Chain | Residue | Details |
| A | GLU142 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXK |
| Chain | Residue | Details |
| A | LYS167 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | SITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1 |
| Chain | Residue | Details |
| A | TRP137 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 329 |
| Chain | Residue | Details |
| A | HIS62 | proton acceptor, proton donor |
| A | LYS71 | electrostatic stabiliser |
| A | TYR131 | proton acceptor, proton donor, proton relay |
| A | ASP168 | electrostatic stabiliser, increase acidity, increase basicity |
