eF-site ID 4r68-C PDB Code 4r68 Chain C 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 C:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK DYNVTANSKLVIITAGALNLVQRNVNIFKFIIPNVVKYSP NCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSAR FRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGV SLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTS WAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFL SVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKE LQF Description Functional site 1) chain C residue 28 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 2) chain C residue 29 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 3) chain C residue 30 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 4) chain C residue 51 type sequence D description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 5) chain C residue 52 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 6) chain C residue 53 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 7) chain C residue 94 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 8) chain C residue 95 type sequence A description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 9) chain C residue 96 type sequence G description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 10) chain C residue 115 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 11) chain C residue 119 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 12) chain C residue 135 type sequence V description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 13) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 14) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 15) chain C residue 247 type sequence T description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 16) chain C residue 251 type sequence I description BINDING SITE FOR RESIDUE NAI C 801 source : AC7 17) chain C residue 147 type sequence W description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 18) chain C residue 151 type sequence G description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 19) chain C residue 152 type sequence F description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 20) chain C residue 153 type sequence P description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 21) chain C residue 154 type sequence K description BINDING SITE FOR RESIDUE EPE C 802 source : AC8 22) chain C residue 137 type sequence N description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 23) chain C residue 165 type sequence D description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 24) chain C residue 168 type sequence R description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 25) chain C residue 192 type sequence H description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 26) chain C residue 193 type sequence G description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 27) chain C residue 194 type sequence D description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 28) chain C residue 237 type sequence A description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 29) chain C residue 238 type sequence Y description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 30) chain C residue 241 type sequence I description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 31) chain C residue 247 type sequence T description BINDING SITE FOR RESIDUE W31 C 803 source : AC9 32) chain C residue 192 type ACT_SITE sequence H description Proton acceptor source Swiss-Prot : SWS_FT_FI1 33) chain C residue 28 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11276087 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 137 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 35) chain C residue 168 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 36) chain C residue 247 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 37) 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 38) chain C residue 4 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 40) chain C residue 317 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI5 41) chain C residue 9 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI6 42) chain C residue 13 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 43) chain C residue 80 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 44) chain C residue 125 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI7 45) chain C residue 17 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 46) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI9 47) chain C residue 223 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 48) chain C residue 231 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 49) chain C residue 242 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI10 50) chain C residue 238 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P06151 source Swiss-Prot : SWS_FT_FI11 51) chain C residue 308 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 52) chain C residue 321 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P04642 source Swiss-Prot : SWS_FT_FI12 53) 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 54) 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

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