eF-site ID 4zz9-B PDB Code 4zz9 Chain B click to enlarge Title Crystal structure of T75S mutant of Triosephosphate isomerase from Plasmodium falciparum Classification ISOMERASE Compound Triosephosphate isomerase Source Plasmodium falciparum (TPIS_PLAFA) Sequence B:  ARKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVV FPVSVHYDHTRKLLQSKFSTGIQNVSKFGNGSYSGEVSAE IAKDLNIEYVIIGHFERRKYFHETDEDVREKLQASLKNNL KAVVCFGESLEQREQNKTIEVITKQVKAFVDLIDNFDNVI LVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQA NQIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFV DIIKSAM Description Functional site 1) chain B residue 76 type sequence G description binding site for residue EDO A 303 source : AC3 2) chain B residue 10 type sequence N description binding site for residue EDO B 301 source : AC5 3) chain B residue 12 type sequence K description binding site for residue EDO B 301 source : AC5 4) chain B residue 95 type sequence H description binding site for residue EDO B 301 source : AC5 5) chain B residue 230 type sequence L description binding site for residue EDO B 301 source : AC5 6) chain B residue 231 type sequence V description binding site for residue EDO B 301 source : AC5 7) chain B residue 232 type sequence G description binding site for residue EDO B 301 source : AC5 8) chain B residue 5 type sequence Y description binding site for residue NA B 302 source : AC6 9) chain B residue 221 type sequence I description binding site for residue NA B 302 source : AC6 10) chain B residue 223 type sequence Q description binding site for residue NA B 302 source : AC6 11) chain B residue 226 type sequence I description binding site for residue NA B 302 source : AC6 12) chain B residue 232 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0000312|PDB:1LZO, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1M7P, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI source Swiss-Prot : SWS_FT_FI7 13) chain B residue 230 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI source Swiss-Prot : SWS_FT_FI6 14) chain B residue 12 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1LZO, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI source Swiss-Prot : SWS_FT_FI4 15) chain B residue 171 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:2VFI source Swiss-Prot : SWS_FT_FI5 16) chain B residue 95 type ACT_SITE sequence H description Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 165 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 10 type BINDING sequence N description BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:2VFI source Swiss-Prot : SWS_FT_FI3

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