eF-site ID 4r68-A PDB Code 4r68 Chain A click to enlarge Title Lactate Dehydrogenase in complex with inhibitor compound 31 Classification OXIDOREDUCTASE Compound L-lactate dehydrogenase A chain Source Homo sapiens (Human) (LDHA_HUMAN) Sequence A:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF Description Functional site 1) chain A residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 2) chain A residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 3) chain A residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 4) chain A residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 5) chain A residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 6) chain A residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 7) chain A residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 8) chain A residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 9) chain A residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 10) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 11) chain A residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 12) chain A residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 13) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 14) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 15) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI A 801 source : AC1 16) chain A residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 17) chain A residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 18) chain A residue 152 type sequence F description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 19) chain A residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 20) chain A residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE A 802 source : AC2 21) chain A residue 105 type sequence R description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 22) chain A residue 108 type sequence L description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 23) chain A residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 24) chain A residue 164 type sequence L description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 25) chain A residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 26) chain A residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 27) chain A residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 28) chain A residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 29) chain A residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 30) chain A residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 31) chain A residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 32) chain A residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 33) chain A residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 A 803 source : AC3 34) chain A residue 283 type sequence K description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 35) chain A residue 242 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 36) chain A residue 243 type sequence L description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 37) chain A residue 244 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 38) chain A residue 245 type sequence G description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 39) chain A residue 189-195 type prosite sequence LGEHGDS description L_LDH L-lactate dehydrogenase active site. LGEHGDS source prosite : PS00064 40) chain A residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 41) chain A residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 42) chain A residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 46) chain A residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 1 type MOD_RES sequence A description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 50) chain A residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 51) chain A residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 54) chain A residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 55) chain A residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 56) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 57) chain A residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 58) chain A residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 59) chain A residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 60) chain A residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 61) chain A residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 62) chain A residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 63) chain A residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 64) chain A residue 56 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI14

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