eF-site ID 5vmp-ABCD PDB Code 5vmp Chain A, B, C, D click to enlarge Title Crystal Structure of Human KDM4 with Small Molecule Inhibitor QC5714 Classification OXIDOREDUCTASE/INHIBITOR Compound Lysine-specific demethylase 4A Source Homo sapiens (Human) (KDM4A_HUMAN) Sequence A:  SETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGL AKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQ YNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKN LTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKES GITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGE PKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTL ISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFN CAESTNFATRRWIEYGKQAVLCSCRVKISMDVFVRKFQPE RYKLWKAGKDNTVIDHTLPTPEAAEFL B:  SETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGL AKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQ YNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKN LTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKES GITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGE PKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTL ISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFN CAESTNFATRRWIEYGKQAVLCSCRVKISMDVFVRKFQPE RYKLWKAGKDNTVIDHTLPTPEAAEFL C:  ARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPK EWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKA MTVREFRKIANSDKYCTPRYFEELERKYWKNLTFNPPIYG ADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNT PYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPP EHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLMLKKY GIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFAT RRWIEYGKQAVLCSCRKISMDVFVRKFQPERYKLWKAGKT VIDHTLPTPEAAEFL D:  SETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGL AKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQ YNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKN LTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKES GVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWY SVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLM LKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAEST NFATRRWIEYGKQAVLCSCRVKISMDVFVRKFQPERYKLW KAGKDNTVIDHTLPTPEAAEF Description Functional site 1) chain A residue 188 type sequence H description binding site for residue NI A 501 source : AC1 2) chain A residue 190 type sequence E description binding site for residue NI A 501 source : AC1 3) chain A residue 276 type sequence H description binding site for residue NI A 501 source : AC1 4) chain A residue 234 type sequence C description binding site for residue ZN A 502 source : AC2 5) chain A residue 240 type sequence H description binding site for residue ZN A 502 source : AC2 6) chain A residue 306 type sequence C description binding site for residue ZN A 502 source : AC2 7) chain A residue 308 type sequence C description binding site for residue ZN A 502 source : AC2 8) chain A residue 73 type sequence Q description binding site for residue 9FJ A 503 source : AC3 9) chain A residue 86 type sequence N description binding site for residue 9FJ A 503 source : AC3 10) chain A residue 132 type sequence Y description binding site for residue 9FJ A 503 source : AC3 11) chain A residue 177 type sequence Y description binding site for residue 9FJ A 503 source : AC3 12) chain A residue 184 type sequence S description binding site for residue 9FJ A 503 source : AC3 13) chain A residue 185 type sequence F description binding site for residue 9FJ A 503 source : AC3 14) chain A residue 188 type sequence H description binding site for residue 9FJ A 503 source : AC3 15) chain A residue 198 type sequence N description binding site for residue 9FJ A 503 source : AC3 16) chain A residue 206 type sequence K description binding site for residue 9FJ A 503 source : AC3 17) chain A residue 208 type sequence W description binding site for residue 9FJ A 503 source : AC3 18) chain A residue 240 type sequence H description binding site for residue 9FJ A 503 source : AC3 19) chain A residue 276 type sequence H description binding site for residue 9FJ A 503 source : AC3 20) chain B residue 188 type sequence H description binding site for residue NI B 501 source : AC4 21) chain B residue 190 type sequence E description binding site for residue NI B 501 source : AC4 22) chain B residue 276 type sequence H description binding site for residue NI B 501 source : AC4 23) chain B residue 234 type sequence C description binding site for residue ZN B 502 source : AC5 24) chain B residue 240 type sequence H description binding site for residue ZN B 502 source : AC5 25) chain B residue 306 type sequence C description binding site for residue ZN B 502 source : AC5 26) chain B residue 308 type sequence C description binding site for residue ZN B 502 source : AC5 27) chain B residue 86 type sequence N description binding site for residue 9FJ B 503 source : AC6 28) chain B residue 132 type sequence Y description binding site for residue 9FJ B 503 source : AC6 29) chain B residue 184 type sequence S description binding site for residue 9FJ B 503 source : AC6 30) chain B residue 185 type sequence F description binding site for residue 9FJ B 503 source : AC6 31) chain B residue 188 type sequence H description binding site for residue 9FJ B 503 source : AC6 32) chain B residue 198 type sequence N description binding site for residue 9FJ B 503 source : AC6 33) chain B residue 206 type sequence K description binding site for residue 9FJ B 503 source : AC6 34) chain B residue 240 type sequence H description binding site for residue 9FJ B 503 source : AC6 35) chain B residue 241 type sequence K description binding site for residue 9FJ B 503 source : AC6 36) chain B residue 276 type sequence H description binding site for residue 9FJ B 503 source : AC6 37) chain C residue 188 type sequence H description binding site for residue NI C 501 source : AC7 38) chain C residue 190 type sequence E description binding site for residue NI C 501 source : AC7 39) chain C residue 276 type sequence H description binding site for residue NI C 501 source : AC7 40) chain C residue 234 type sequence C description binding site for residue ZN C 502 source : AC8 41) chain C residue 240 type sequence H description binding site for residue ZN C 502 source : AC8 42) chain C residue 306 type sequence C description binding site for residue ZN C 502 source : AC8 43) chain C residue 308 type sequence C description binding site for residue ZN C 502 source : AC8 44) chain C residue 73 type sequence Q description binding site for residue 9FJ C 503 source : AC9 45) chain C residue 86 type sequence N description binding site for residue 9FJ C 503 source : AC9 46) chain C residue 132 type sequence Y description binding site for residue 9FJ C 503 source : AC9 47) chain C residue 184 type sequence S description binding site for residue 9FJ C 503 source : AC9 48) chain C residue 185 type sequence F description binding site for residue 9FJ C 503 source : AC9 49) chain C residue 188 type sequence H description binding site for residue 9FJ C 503 source : AC9 50) chain C residue 206 type sequence K description binding site for residue 9FJ C 503 source : AC9 51) chain C residue 208 type sequence W description binding site for residue 9FJ C 503 source : AC9 52) chain C residue 240 type sequence H description binding site for residue 9FJ C 503 source : AC9 53) chain C residue 276 type sequence H description binding site for residue 9FJ C 503 source : AC9 54) chain D residue 188 type sequence H description binding site for residue NI D 501 source : AD1 55) chain D residue 190 type sequence E description binding site for residue NI D 501 source : AD1 56) chain D residue 276 type sequence H description binding site for residue NI D 501 source : AD1 57) chain D residue 234 type sequence C description binding site for residue ZN D 502 source : AD2 58) chain D residue 240 type sequence H description binding site for residue ZN D 502 source : AD2 59) chain D residue 306 type sequence C description binding site for residue ZN D 502 source : AD2 60) chain D residue 308 type sequence C description binding site for residue ZN D 502 source : AD2 61) chain D residue 86 type sequence N description binding site for residue 9FJ D 503 source : AD3 62) chain D residue 132 type sequence Y description binding site for residue 9FJ D 503 source : AD3 63) chain D residue 184 type sequence S description binding site for residue 9FJ D 503 source : AD3 64) chain D residue 185 type sequence F description binding site for residue 9FJ D 503 source : AD3 65) chain D residue 188 type sequence H description binding site for residue 9FJ D 503 source : AD3 66) chain D residue 206 type sequence K description binding site for residue 9FJ D 503 source : AD3 67) chain D residue 240 type sequence H description binding site for residue 9FJ D 503 source : AD3 68) chain D residue 241 type sequence K description binding site for residue 9FJ D 503 source : AD3 69) chain D residue 276 type sequence H description binding site for residue 9FJ D 503 source : AD3 70) chain A residue 170 type catalytic sequence G description 370 source MCSA : MCSA1 71) chain A residue 177 type catalytic sequence Y description 370 source MCSA : MCSA1 72) chain A residue 188 type catalytic sequence H description 370 source MCSA : MCSA1 73) chain A residue 190 type catalytic sequence E description 370 source MCSA : MCSA1 74) chain A residue 276 type catalytic sequence H description 370 source MCSA : MCSA1 75) chain A residue 288 type catalytic sequence S description 370 source MCSA : MCSA1 76) chain B residue 170 type catalytic sequence G description 370 source MCSA : MCSA2 77) chain B residue 177 type catalytic sequence Y description 370 source MCSA : MCSA2 78) chain B residue 188 type catalytic sequence H description 370 source MCSA : MCSA2 79) chain B residue 190 type catalytic sequence E description 370 source MCSA : MCSA2 80) chain B residue 276 type catalytic sequence H description 370 source MCSA : MCSA2 81) chain B residue 288 type catalytic sequence S description 370 source MCSA : MCSA2 82) chain C residue 170 type catalytic sequence G description 370 source MCSA : MCSA3 83) chain C residue 177 type catalytic sequence Y description 370 source MCSA : MCSA3 84) chain C residue 188 type catalytic sequence H description 370 source MCSA : MCSA3 85) chain C residue 190 type catalytic sequence E description 370 source MCSA : MCSA3 86) chain C residue 276 type catalytic sequence H description 370 source MCSA : MCSA3 87) chain C residue 288 type catalytic sequence S description 370 source MCSA : MCSA3 88) chain D residue 177 type catalytic sequence Y description 370 source MCSA : MCSA4 89) chain D residue 188 type catalytic sequence H description 370 source MCSA : MCSA4 90) chain D residue 190 type catalytic sequence E description 370 source MCSA : MCSA4 91) chain D residue 276 type catalytic sequence H description 370 source MCSA : MCSA4 92) chain D residue 288 type catalytic sequence S description 370 source MCSA : MCSA4 93) chain A residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 94) chain B residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 95) chain C residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 96) chain D residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 97) chain A residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 98) chain D residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 99) chain D residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 100) chain D residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 101) chain A residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 102) chain A residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 103) chain B residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 104) chain B residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 105) chain B residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 106) chain C residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 107) chain C residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 108) chain C residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 109) chain A residue 188 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 110) chain A residue 276 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 111) chain B residue 188 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 112) chain B residue 276 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 113) chain C residue 188 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 114) chain C residue 276 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 115) chain D residue 188 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 116) chain D residue 276 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI2 117) chain A residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 118) chain B residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 119) chain C residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 120) chain D residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 121) chain A residue 234 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 122) chain C residue 240 type BINDING sequence H description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 123) chain C residue 306 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 124) chain C residue 308 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 125) chain D residue 234 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 126) chain D residue 240 type BINDING sequence H description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 127) chain D residue 306 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 128) chain D residue 308 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 129) chain A residue 240 type BINDING sequence H description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 130) chain A residue 306 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 131) chain A residue 308 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 132) chain B residue 234 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 133) chain B residue 240 type BINDING sequence H description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 134) chain B residue 306 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 135) chain B residue 308 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4 136) chain C residue 234 type BINDING sequence C description BINDING => ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32, ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39, ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G, ECO:0007744|PDB:5F5I source Swiss-Prot : SWS_FT_FI4

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