eF-site ID 1i32-C PDB Code 1i32 Chain C click to enlarge Title LEISHMANIA MEXICANA GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE IN COMPLEX WITH INHIBITORS Classification OXIDOREDUCTASE Compound GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE Source Leishmania mexicana (G3PG_LEIME) Sequence C:  APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMS TNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVV NGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKA EGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHV VSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKA AQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNL PGEKRFFKVVSWYDNEWAYSHRVVDLVRYMAAKDAASS Description Functional site 1) chain C residue 8 type sequence N description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 2) chain C residue 9 type sequence G description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 3) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 4) chain C residue 37 type sequence V description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 5) chain C residue 38 type sequence D description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 6) chain C residue 39 type sequence M description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 7) chain C residue 40 type sequence S description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 8) chain C residue 90 type sequence A description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 9) chain C residue 91 type sequence Q description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 10) chain C residue 92 type sequence R description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 11) chain C residue 111 type sequence T description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 12) chain C residue 208 type sequence L description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 13) chain C residue 167 type ACT_SITE sequence T description Nucleophile source Swiss-Prot : SWS_FT_FI1 14) chain C residue 13 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 39 type BINDING sequence M description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 16) chain C residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 17) chain C residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 18) chain C residue 336 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 19) chain C residue 198 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 20) chain C residue 227 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 250 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain C residue 166 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain C residue 195 type SITE sequence S description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4

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