eF-site ID 4ajl-B PDB Code 4ajl Chain B click to enlarge Title rat LDHA in complex with 3-(ethylcarbamoylamino)-N-(2-methyl-1,3- benzothiazol-6-yl)propanamide Classification OXIDOREDUCTASE/INHIBITOR Compound L-LACTATE DEHYDROGENASE A CHAIN Source Rattus norvegicus (Rat) (LDHA_RAT) Sequence B:  ALKDQLIVNLLKQVPQNKITVVGVGAVGMACAISILMKDL ADELALVDVIEDKLKGEMMDLQHGSLFLKTPKIVSSKDYS VTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNV VKYSPQCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCN LDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGV NVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKL KGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGIK EDVFLSVPCILGQNGISDVVKVTLTPDEEARLKKSADTLW GIQKELQF Description Functional site 1) chain B residue 201 type sequence S description BINDING SITE FOR RESIDUE GOL C 1334 source : AC2 2) chain B residue 202 type sequence G description BINDING SITE FOR RESIDUE GOL C 1334 source : AC2 3) chain B residue 204 type sequence N description BINDING SITE FOR RESIDUE GOL C 1334 source : AC2 4) chain B residue 207 type sequence G description BINDING SITE FOR RESIDUE GOL C 1334 source : AC2 5) chain B residue 40 type sequence M description BINDING SITE FOR RESIDUE GOL B 1332 source : AC3 6) chain B residue 42 type sequence D description BINDING SITE FOR RESIDUE GOL B 1332 source : AC3 7) chain B residue 70 type sequence F description BINDING SITE FOR RESIDUE GOL B 1332 source : AC3 8) chain B residue 71 type sequence L description BINDING SITE FOR RESIDUE GOL B 1332 source : AC3 9) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 10) chain B residue 52 type sequence V description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 11) chain B residue 94 type sequence T description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 12) chain B residue 95 type sequence A description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 13) chain B residue 96 type sequence G description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 14) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 15) chain B residue 119 type sequence I description BINDING SITE FOR RESIDUE 88W B 1333 source : AC9 16) chain B residue 170 type sequence R description BINDING SITE FOR RESIDUE MLI B 1334 source : BC5 17) chain B residue 185 type sequence H description BINDING SITE FOR RESIDUE MLI B 1334 source : BC5 18) chain B residue 187 type sequence W description BINDING SITE FOR RESIDUE MLI B 1334 source : BC5 19) chain B residue 269 type sequence V description BINDING SITE FOR RESIDUE MLI B 1334 source : BC5 20) chain B residue 99 type sequence Q description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 21) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 22) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 23) chain B residue 168 type sequence R description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 24) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 25) chain B residue 237 type sequence A description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 26) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE MLI B 1335 source : BC6 27) chain B residue 183 type sequence S description BINDING SITE FOR RESIDUE MLI C 1338 source : BC8 28) chain B residue 185 type sequence H description BINDING SITE FOR RESIDUE MLI C 1338 source : BC8 29) chain B residue 192 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 31) chain B residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 32) 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 33) chain B residue 137 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 34) chain B residue 168 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 35) chain B residue 247 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 28 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 98 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 105 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 40) chain B residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 41) chain B residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 42) chain B residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 43) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 44) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 45) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI6 46) chain B residue 212 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI7 47) chain B residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 48) chain B residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 49) chain B residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 50) chain B residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI9

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