eF-site ID 4r68-B PDB Code 4r68 Chain B 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 B:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD TLWGIQKELQF Description Functional site 1) chain B residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 2) chain B residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 3) chain B residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 4) chain B residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 5) chain B residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 6) chain B residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 7) chain B residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 8) chain B residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 9) chain B residue 98 type sequence R description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 10) chain B residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 11) chain B residue 119 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 12) chain B residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 13) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 14) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 15) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 16) chain B residue 251 type sequence I description BINDING SITE FOR RESIDUE NAI B 801 source : AC4 17) chain B residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 18) chain B residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 19) chain B residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 20) chain B residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE B 802 source : AC5 21) chain B residue 105 type sequence R description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 22) chain B residue 108 type sequence L description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 23) chain B residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 24) chain B residue 164 type sequence L description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 25) chain B residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 26) chain B residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 27) chain B residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 28) chain B residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 29) chain B residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 30) chain B residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 31) chain B residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 32) chain B residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 33) chain B residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 B 803 source : AC6 34) chain B residue 55 type sequence D description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 35) chain B residue 56 type sequence K description BINDING SITE FOR RESIDUE EPE D 803 source : BC3 36) chain B residue 185 type sequence H description BINDING SITE FOR RESIDUE SO4 D 804 source : BC4 37) chain B residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 38) chain B residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 98 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 105 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 41) chain B residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 42) chain B residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 43) chain B residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 44) chain B 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 45) chain B residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 46) chain B residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 47) chain B residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 48) chain B residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 49) chain B residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 50) chain B residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 51) chain B residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 52) chain B residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 53) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 54) chain B residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 55) chain B residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 56) chain B residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 57) chain B residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 58) chain B residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 59) chain B residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 60) chain B residue 309 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 61) chain B 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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