eF-site ID 4aji-B PDB Code 4aji Chain B click to enlarge Title rat LDHA in complex with 2-((3,4-dimethoxyphenyl)methyl))propanedioic acid Classification OXIDOREDUCTASE/INHIBITOR Compound L-LACTATE DEHYDROGENASE A CHAIN Source Rattus norvegicus (Rat) (LDHA_RAT) Sequence B:  ALKDQLIVNLLKEEQVPQNKITVVGVGAVGMACAISILMK DLADELALVDVIEDKLKGEMMDLQHGSLFLKTPKIVSSKD YSVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIP NVVKYSPQCKLLIVSNPVDILTYVAWKISGFPKNRVIGSG CNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWS GVNVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVI KLKGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYG IKEDVFLSVPCILGQNGISDVVKVTLTPDEEARLKKSADT LWGIQKELQF Description (1)  L-LACTATE DEHYDROGENASE A CHAIN (E.C.1.1.1.27) Functional site 1) chain B residue 30 type sequence V description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 2) chain B residue 94 type sequence T description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 3) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 4) chain B residue 99 type sequence Q description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 5) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 6) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 7) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 8) chain B residue 168 type sequence R description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 9) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 10) chain B residue 237 type sequence A description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 11) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE 88R B 1332 source : AC2 12) chain B residue 192 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 14) chain B residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 15) chain B residue 56 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI11 16) chain B residue 137 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 168 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 247 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 28 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 98 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 105 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI9 23) chain B residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 24) chain B residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 28) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 212 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI7 31) chain B residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 32) chain B residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 33) chain B residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8

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