eF-site ID 1i32-ABCD PDB Code 1i32 Chain A, B, C, D 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 A:  APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMS TNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVV NGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKA EGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHV VSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKA AQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNL PGEKRFFKVVSWYDNEWAYSHRVVDLVRYMAAKDAASS B:  APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMS TNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVV NGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKA EGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHV VSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKA AQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNL PGEKRFFKVVSWYDNEWAYSHRVVDLVRYMAAKDAASS C:  APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMS TNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVV NGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKA EGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHV VSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKA AQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNL PGEKRFFKVVSWYDNEWAYSHRVVDLVRYMAAKDAASS D:  APIKVGINGFGRIGRMVFQAICDQGLIGTEIDVVAVVDMS TNAEYFAYQMKHDTVHGRPKYTVEAVKSSPSVETADVLVV NGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLKA EGHIKGGAKKVVISAPASGGAKTIVMGVNQHEYSPASHHV VSNASCTTNCLAPIVHVLTKENFGIETGLMTTIHSYTATQ KTVDGVSLKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDKAIKKA AQTYMKGILGFTDEELVSADFINDNRSSVYDSKATLQNNL PGEKRFFKVVSWYDNEWAYSHRVVDLVRYMAAKDAASS Description Functional site 1) chain A residue 8 type sequence N description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 2) chain A residue 9 type sequence G description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 3) chain A residue 11 type sequence G description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 4) chain A residue 37 type sequence V description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 5) chain A residue 38 type sequence D description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 6) chain A residue 39 type sequence M description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 7) chain A residue 40 type sequence S description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 8) chain A residue 90 type sequence A description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 9) chain A residue 91 type sequence Q description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 10) chain A residue 92 type sequence R description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 11) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 12) chain A residue 113 type sequence L description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 13) chain B residue 206 type sequence V description BINDING SITE FOR RESIDUE NMD A 361 source : AC1 14) chain A residue 206 type sequence V description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 15) chain B residue 8 type sequence N description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 16) chain B residue 9 type sequence G description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 17) chain B residue 11 type sequence G description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 18) chain B residue 37 type sequence V description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 19) chain B residue 38 type sequence D description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 20) chain B residue 39 type sequence M description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 21) chain B residue 40 type sequence S description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 22) chain B residue 90 type sequence A description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 23) chain B residue 91 type sequence Q description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 24) chain B residue 92 type sequence R description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 25) chain B residue 111 type sequence T description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 26) chain B residue 113 type sequence L description BINDING SITE FOR RESIDUE NMD B 362 source : AC2 27) chain C residue 8 type sequence N description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 28) chain C residue 9 type sequence G description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 29) chain C residue 11 type sequence G description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 30) chain C residue 37 type sequence V description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 31) chain C residue 38 type sequence D description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 32) chain C residue 39 type sequence M description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 33) chain C residue 40 type sequence S description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 34) chain C residue 90 type sequence A description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 35) chain C residue 91 type sequence Q description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 36) chain C residue 92 type sequence R description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 37) chain C residue 111 type sequence T description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 38) chain D residue 208 type sequence L description BINDING SITE FOR RESIDUE NMD C 363 source : AC3 39) chain C residue 208 type sequence L description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 40) chain D residue 8 type sequence N description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 41) chain D residue 9 type sequence G description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 42) chain D residue 11 type sequence G description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 43) chain D residue 38 type sequence D description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 44) chain D residue 39 type sequence M description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 45) chain D residue 40 type sequence S description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 46) chain D residue 90 type sequence A description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 47) chain D residue 91 type sequence Q description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 48) chain D residue 92 type sequence R description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 49) chain D residue 111 type sequence T description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 50) chain D residue 113 type sequence L description BINDING SITE FOR RESIDUE NMD D 364 source : AC4 51) chain A residue 164-171 type prosite sequence ASCTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 52) chain A residue 167 type ACT_SITE sequence T description Nucleophile source Swiss-Prot : SWS_FT_FI1 53) chain B residue 167 type ACT_SITE sequence T description Nucleophile source Swiss-Prot : SWS_FT_FI1 54) chain C residue 167 type ACT_SITE sequence T description Nucleophile source Swiss-Prot : SWS_FT_FI1 55) chain D residue 167 type ACT_SITE sequence T description Nucleophile source Swiss-Prot : SWS_FT_FI1 56) chain A residue 13 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 336 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 13 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 39 type BINDING sequence M description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 60) chain C residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 61) chain C residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 62) chain C residue 336 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 63) chain D residue 13 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 64) chain D residue 39 type BINDING sequence M description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 65) chain D residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 66) chain D residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 67) chain A residue 39 type BINDING sequence M description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 68) chain D residue 336 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 69) chain A residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 70) chain A residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 336 type BINDING sequence E description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 13 type BINDING sequence I description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 39 type BINDING sequence M description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 74) chain B residue 92 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 75) chain B residue 135 type BINDING sequence A description BINDING => ECO:0000269|PubMed:7578111, ECO:0000269|PubMed:9571030 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 166 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 77) chain C residue 198 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 78) chain C residue 227 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 79) chain C residue 250 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 80) chain D residue 166 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 81) chain D residue 198 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 82) chain D residue 227 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 83) chain D residue 250 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 84) chain A residue 198 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 227 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 86) chain A residue 250 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 87) chain B residue 166 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 88) chain B residue 198 type BINDING sequence A description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 227 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 90) chain B residue 250 type BINDING sequence V description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 91) chain C residue 166 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 92) chain A residue 195 type SITE sequence S description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 93) chain B residue 195 type SITE sequence S description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 94) chain C residue 195 type SITE sequence S description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4 95) chain D residue 195 type SITE sequence S description Activates thiol group during catalysis source Swiss-Prot : SWS_FT_FI4

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