eF-site ID 5vmp-A PDB Code 5vmp Chain A 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 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 A residue 170 type catalytic sequence G description 370 source MCSA : MCSA1 21) chain A residue 177 type catalytic sequence Y description 370 source MCSA : MCSA1 22) chain A residue 188 type catalytic sequence H description 370 source MCSA : MCSA1 23) chain A residue 190 type catalytic sequence E description 370 source MCSA : MCSA1 24) chain A residue 276 type catalytic sequence H description 370 source MCSA : MCSA1 25) chain A residue 288 type catalytic sequence S description 370 source MCSA : MCSA1 26) chain A residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 27) chain A residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 30) 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 31) 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 32) chain A residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 33) 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 34) 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 35) 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 36) 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

Display surface Download Links