eF-site ID 4ajl-A PDB Code 4ajl Chain A 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 A:  ALKDQLIVNLLKQVPQNKITVVGVGAVGMACAISILMKDL ADELALVDVIEDKLKGEMMDLQHGSLFLKTPKIVSSKDYS VTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNV VKYSPQCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCN LDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGV NVAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKL KGYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGIK EDVFLSVPCILGQNGISDVVKVTLTPDEEARLKKSADTLW GIQKELQF Description Functional site 1) chain A residue 40 type sequence M description BINDING SITE FOR RESIDUE GOL B 1332 source : AC3 2) chain A residue 201 type sequence S description BINDING SITE FOR RESIDUE GOL A 1332 source : AC5 3) chain A residue 202 type sequence G description BINDING SITE FOR RESIDUE GOL A 1332 source : AC5 4) chain A residue 204 type sequence N description BINDING SITE FOR RESIDUE GOL A 1332 source : AC5 5) chain A residue 207 type sequence G description BINDING SITE FOR RESIDUE GOL A 1332 source : AC5 6) chain A residue 209 type sequence S description BINDING SITE FOR RESIDUE GOL A 1332 source : AC5 7) chain A residue 26 type sequence G description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 8) chain A residue 28 type sequence G description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 9) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 10) chain A residue 52 type sequence V description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 11) chain A residue 94 type sequence T description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 12) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 13) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 14) chain A residue 118 type sequence F description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 15) chain A residue 119 type sequence I description BINDING SITE FOR RESIDUE 88W A 1333 source : AC8 16) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 17) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 18) chain A residue 164 type sequence L description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 19) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 20) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 21) chain A residue 237 type sequence A description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 22) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE MLI A 1334 source : BC4 23) chain A residue 170 type sequence R description BINDING SITE FOR RESIDUE MLI A 1335 source : BC7 24) chain A residue 185 type sequence H description BINDING SITE FOR RESIDUE MLI A 1335 source : BC7 25) chain A residue 269 type sequence V description BINDING SITE FOR RESIDUE MLI A 1335 source : BC7 26) chain A residue 183 type sequence S description BINDING SITE FOR RESIDUE MLI D 1335 source : CC1 27) chain A residue 185 type sequence H description BINDING SITE FOR RESIDUE MLI D 1335 source : CC1 28) chain A residue 189-195 type prosite sequence LGEHGDS description L_LDH L-lactate dehydrogenase active site. LGEHGDS source prosite : PS00064 29) chain A residue 192 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 31) chain A residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 32) chain A 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 A residue 28 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 98 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 105 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 137 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 168 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 247 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 40) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 42) chain A residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 43) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 44) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI6 46) chain A residue 212 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI7 47) chain A residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 48) chain A residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 49) chain A residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 50) chain A residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI9

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