eF-site ID 4qo8-C PDB Code 4qo8 Chain C click to enlarge Title Lactate Dehydrogenase A in complex with substituted 3-Hydroxy-2-mercaptocyclohex-2-enone compound 104 Classification oxidoreductase/oxidoreductase inhibitor Compound L-lactate dehydrogenase A chain Source Homo sapiens (Human) (LDHA_HUMAN) Sequence C:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF Description Functional site 1) chain C residue 185 type sequence H description BINDING SITE FOR RESIDUE SO4 A 803 source : AC3 2) chain C residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 3) chain C residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 4) chain C residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 5) chain C residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 6) chain C residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 7) chain C residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 8) chain C residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 9) chain C residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 10) chain C residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 11) chain C residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 12) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 13) chain C residue 136 type sequence S description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 14) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 15) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 16) chain C residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC9 17) chain C residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE C 802 source : BC1 18) chain C residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE C 802 source : BC1 19) chain C residue 152 type sequence F description BINDING SITE FOR RESIDUE EPE C 802 source : BC1 20) chain C residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE C 802 source : BC1 21) chain C residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE C 802 source : BC1 22) chain C residue 170 type sequence R description BINDING SITE FOR RESIDUE SO4 C 803 source : BC2 23) chain C residue 185 type sequence H description BINDING SITE FOR RESIDUE SO4 C 803 source : BC2 24) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 25) chain C residue 165 type sequence D description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 26) chain C residue 168 type sequence R description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 27) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 28) chain C residue 193 type sequence G description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 29) chain C residue 237 type sequence A description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 30) chain C residue 238 type sequence Y description BINDING SITE FOR RESIDUE 36U C 804 source : BC3 31) chain C residue 101 type sequence E description BINDING SITE FOR RESIDUE NAI D 801 source : BC4 32) chain C residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 33) chain C residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 34) chain C residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 35) chain C residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 36) chain C residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 37) chain C residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 38) chain C residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 39) chain C residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 40) chain C 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 41) chain C residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 42) chain C residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 43) chain C residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 44) chain C residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 45) chain C residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 46) chain C residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 47) chain C 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 C residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 49) chain C residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 50) chain C residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 51) chain C residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 52) chain C residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 53) chain C residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 54) chain C residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 55) chain C residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 56) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9

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