eF-site ID 4aji-D PDB Code 4aji Chain D 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 D:  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 D residue 30 type sequence V description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 2) chain D residue 94 type sequence T description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 3) chain D residue 99 type sequence Q description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 4) chain D residue 105 type sequence R description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 5) chain D residue 135 type sequence V description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 6) chain D residue 137 type sequence N description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 7) chain D residue 168 type sequence R description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 8) chain D residue 192 type sequence H description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 9) chain D residue 237 type sequence A description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 10) chain D residue 247 type sequence T description BINDING SITE FOR RESIDUE 88R D 1332 source : AC4 11) chain D residue 192 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain D residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 13) chain D residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 14) chain D 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 15) chain D residue 28 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 98 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 105 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 137 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 19) chain D residue 168 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain D residue 247 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 21) chain D residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI9 22) chain D residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 23) chain D residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 24) chain D residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 25) chain D residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 26) chain D residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 27) chain D residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 28) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI6 29) chain D residue 212 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI7 30) chain D residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 31) chain D residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 32) chain D residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8

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