eF-site ID 4aji-A PDB Code 4aji Chain A 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 A:  ALKDQLIVNLLKVPQNKITVVGVGAVGMACAISILMKDLA DELALVDVIEDKLKGEMMDLQHGSLFLKTPKIVSSKDYSV TANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVV KYSPQCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNL DSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGVN VAGVSLKSLNPQLGTDADKEQWKDVHKQVVDSAYEVIKLK GYTSWAIGLSVADLAESIMKNLRRVHPISTMIKGLYGIKE DVFLSVPCILGQNGISDVVKVTLTPDEEARLKKSADTLWG IQKELQF Description Functional site 1) chain A residue 30 type sequence V description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 2) chain A residue 94 type sequence T description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 3) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 4) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 5) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 6) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 7) chain A residue 164 type sequence L description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 8) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 9) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 10) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 11) chain A residue 251 type sequence I description BINDING SITE FOR RESIDUE 88R A 1332 source : AC1 12) chain A residue 189-195 type prosite sequence LGEHGDS description L_LDH L-lactate dehydrogenase active site. LGEHGDS source prosite : PS00064 13) chain A residue 192 type ACT_SITE sequence H description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 15) chain A residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI10 16) 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 17) chain A residue 28 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 98 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 105 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 137 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 168 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 247 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 24) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 25) chain A residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI4 26) chain A residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 28) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00338 source Swiss-Prot : SWS_FT_FI6 30) chain A residue 212 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI7 31) chain A residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 32) chain A residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 33) chain A residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI8 34) chain A residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links