eF-site ID 1rtv-A PDB Code 1rtv Chain A click to enlarge Title RmlC (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) crystal structure from Pseudomonas aeruginosa, apo structure Classification ISOMERASE Compound dTDP-4-dehydrorhamnose 3,5-epimerase Source Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (Q9HU21_PSEAE) Sequence A:  SMAMKATRLAIPDVILFEPRVFGDDRGFFFESYNQRAFEE ACGHPVSFVQDNHSRSARGVLRGLHYQIRQAQGKLVRATL GEVFDVAVDLRRGSPTFGQWVGERLSAENKRQMWIPAGFA HGFVVLSEYAEFLYKTTDFWAPEHERCIVWNDPELKIDWP LQDAPLLSEKDRQGKAFADADCFP Description Functional site 1) chain A residue 59 type sequence R description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 2) chain A residue 62 type sequence H description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 3) chain A residue 71 type sequence K description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 4) chain A residue 89 type sequence R description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 5) chain A residue 118 type sequence H description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 6) chain A residue 131 type sequence Y description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 7) chain A residue 137 type sequence W description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 8) chain A residue 142 type sequence E description BINDING SITE FOR RESIDUE SRT A 182 source : AC1 9) chain A residue 62 type catalytic sequence H description 329 source MCSA : MCSA1 10) chain A residue 71 type catalytic sequence K description 329 source MCSA : MCSA1 11) chain A residue 131 type catalytic sequence Y description 329 source MCSA : MCSA1 12) chain A residue 168 type catalytic sequence D description 329 source MCSA : MCSA1 13) chain A residue 62 type ACT_SITE sequence H description Proton acceptor => ECO:0000305|PubMed:17046787 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 137 type SITE sequence W description Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1 source Swiss-Prot : SWS_FT_FI9 15) chain A residue 47 type BINDING sequence Q description BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXH source Swiss-Prot : SWS_FT_FI4 16) chain A residue 59 type BINDING sequence R description 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 source Swiss-Prot : SWS_FT_FI5 17) chain A residue 71 type BINDING sequence K description 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 source Swiss-Prot : SWS_FT_FI6 18) chain A residue 118 type BINDING sequence H description 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 source Swiss-Prot : SWS_FT_FI6 19) chain A residue 142 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXJ source Swiss-Prot : SWS_FT_FI7 20) chain A residue 167 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXK source Swiss-Prot : SWS_FT_FI8 21) chain A residue 131 type ACT_SITE sequence Y description Proton donor => ECO:0000305|PubMed:17046787 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 23 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXK source Swiss-Prot : SWS_FT_FI3 23) chain A residue 28 type BINDING sequence E description BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXK source Swiss-Prot : SWS_FT_FI3

Display surface Download Links