eF-site ID 6utn-AB PDB Code 6utn Chain A, B click to enlarge Title Native E. coli Glyceraldehyde 3-phosphate dehydrogenase Classification CYTOSOLIC PROTEIN Compound Glyceraldehyde-3-phosphate dehydrogenase Source (A0A0U4BD45_ECOLX) Sequence A:  TIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYX AYXLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVXTG PSKDNTPXFVKGANFDKYAGQDIVSNASXTTNCLAPLAKV INDNFGIIEGLXTTVHATTATQKTVDGPSHKDWRGGRGAS QNIIPSSTGAAKAVGKVLPELNGKLTGXAFRVPTPNVSVV DLTVRLEKAATYEQIKAAVKAAAEGEXKGVLGYTEDDVVS TDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNK VLDLIAHISK B:  TIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYX AYXLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVXTG PSKDNTPXFVKGANFDKYAGQDIVSNASXTTNCLAPLAKV INDNFGIIEGLXTTVHATTATQKTVDGPSHKDWRGGRGAS QNIIPSSTGAAKAVGKVLPELNGKLTGXAFRVPTPNVSVV DLTVRLEKAATYEQIKAAVKAAAEGEXKGVLGYTEDDVVS TDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNK VLDLIAHISK Description (1)  Glyceraldehyde-3-phosphate dehydrogenase (E.C.1.2.1.-) Functional site 1) chain A residue 114 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 2) chain B residue 123 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 3) chain B residue 212 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 4) chain B residue 216 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 5) chain B residue 224 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 6) chain B residue 248 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 7) chain B residue 256 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 8) chain B residue 260 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 9) chain A residue 123 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 10) chain A residue 212 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 11) chain A residue 216 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 12) chain A residue 224 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 13) chain A residue 248 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 14) chain A residue 256 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 15) chain A residue 260 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 16) chain B residue 114 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI10 17) chain A residue 131 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 18) chain A residue 191 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 19) chain A residue 330 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 20) chain B residue 131 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 21) chain B residue 191 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 22) chain B residue 330 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI11 23) chain A residue 77 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 77 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 119 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19542219 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 119 type BINDING sequence T description BINDING => ECO:0000269|PubMed:19542219 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 148 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10978154 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 208 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10978154 source Swiss-Prot : SWS_FT_FI6 29) chain B residue 148 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10978154 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 208 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10978154 source Swiss-Prot : SWS_FT_FI6 31) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00362 source Swiss-Prot : SWS_FT_FI7 32) chain B residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P00362 source Swiss-Prot : SWS_FT_FI7 33) chain A residue 231 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154 source Swiss-Prot : SWS_FT_FI8 34) chain B residue 231 type BINDING sequence R description BINDING => ECO:0000269|PubMed:19542219, ECO:0000269|Ref.18, ECO:0000305|PubMed:10978154 source Swiss-Prot : SWS_FT_FI8 35) chain A residue 176 type SITE sequence H description Activates thiol group during catalysis => ECO:0000269|PubMed:2659073 source Swiss-Prot : SWS_FT_FI9 36) chain B residue 176 type SITE sequence H description Activates thiol group during catalysis => ECO:0000269|PubMed:2659073 source Swiss-Prot : SWS_FT_FI9 37) chain A residue 149 type ACT_SITE sequence X description Nucleophile => ECO:0000305|PubMed:10978154 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 149 type ACT_SITE sequence X description Nucleophile => ECO:0000305|PubMed:10978154 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 33 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 source Swiss-Prot : SWS_FT_FI3 41) chain B residue 33 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 source Swiss-Prot : SWS_FT_FI3 42) chain B residue 313 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 11 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 11 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10978154, ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984, ECO:0000269|Ref.18 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 147-154 type prosite sequence ASXTTNCL description GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL source prosite : PS00071 46) chain A residue 137 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI12 47) chain B residue 137 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI12

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