eF-site ID 4ura-A PDB Code 4ura Chain A click to enlarge Title Crystal structure of human JMJD2A in complex with compound 14a Classification OXIDOREDUCTASE Compound LYSINE-SPECIFIC DEMETHYLASE 4A Source Homo sapiens (Human) (KDM4A_HUMAN) Sequence A:  ESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAG LAKVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFT QYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWK NLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKE SGITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFG EPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMT LISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGF NCAESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRK FQPERYKLWKAGKDNTVIDHTLPTPEAAE Description (1)  LYSINE-SPECIFIC DEMETHYLASE 4A (E.C.1.14.11.-) Functional site 1) chain A residue 188 type sequence H description BINDING SITE FOR RESIDUE NI A 2501 source : AC1 2) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE NI A 2501 source : AC1 3) chain A residue 276 type sequence H description BINDING SITE FOR RESIDUE NI A 2501 source : AC1 4) chain A residue 234 type sequence C description BINDING SITE FOR RESIDUE ZN A 2502 source : AC2 5) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE ZN A 2502 source : AC2 6) chain A residue 306 type sequence C description BINDING SITE FOR RESIDUE ZN A 2502 source : AC2 7) chain A residue 308 type sequence C description BINDING SITE FOR RESIDUE ZN A 2502 source : AC2 8) chain A residue 132 type sequence Y description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 9) chain A residue 177 type sequence Y description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 10) chain A residue 185 type sequence F description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 11) chain A residue 188 type sequence H description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 12) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 13) chain A residue 206 type sequence K description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 14) chain A residue 241 type sequence K description BINDING SITE FOR RESIDUE LEL A 4000 source : AC3 15) chain A residue 170 type sequence G description BINDING SITE FOR RESIDUE EDO A 1353 source : AC7 16) chain A residue 177 type sequence Y description BINDING SITE FOR RESIDUE EDO A 1353 source : AC7 17) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE EDO A 1353 source : AC7 18) chain A residue 196 type sequence S description BINDING SITE FOR RESIDUE EDO A 1353 source : AC7 19) chain A residue 288 type sequence S description BINDING SITE FOR RESIDUE EDO A 1353 source : AC7 20) chain A residue 227 type sequence F description BINDING SITE FOR RESIDUE SO4 A 1354 source : AC8 21) chain A residue 228 type sequence P description BINDING SITE FOR RESIDUE SO4 A 1354 source : AC8 22) chain A residue 229 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1354 source : AC8 23) chain A residue 230 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1354 source : AC8 24) chain A residue 105 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1354 source : AC9 25) chain A residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5 26) chain A residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 29) 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 30) 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 31) chain A residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 32) 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 33) 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 34) 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 35) 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 36) chain A residue 170 type catalytic sequence G description 370 source MCSA : MCSA1 37) chain A residue 177 type catalytic sequence Y description 370 source MCSA : MCSA1 38) chain A residue 188 type catalytic sequence H description 370 source MCSA : MCSA1 39) chain A residue 190 type catalytic sequence E description 370 source MCSA : MCSA1 40) chain A residue 276 type catalytic sequence H description 370 source MCSA : MCSA1 41) chain A residue 288 type catalytic sequence S description 370 source MCSA : MCSA1

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