eF-site ID 4ura-B PDB Code 4ura Chain B 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 B:  PSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVP PKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQK KAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNP PIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIE GVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWY SVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLM LKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAEST NFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPERY KLWKAGKDNTVIDHTLPTPEAAEF Description Functional site 1) chain B residue 188 type sequence H description BINDING SITE FOR RESIDUE NI B 2501 source : AC4 2) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE NI B 2501 source : AC4 3) chain B residue 276 type sequence H description BINDING SITE FOR RESIDUE NI B 2501 source : AC4 4) chain B residue 234 type sequence C description BINDING SITE FOR RESIDUE ZN B 2502 source : AC5 5) chain B residue 240 type sequence H description BINDING SITE FOR RESIDUE ZN B 2502 source : AC5 6) chain B residue 306 type sequence C description BINDING SITE FOR RESIDUE ZN B 2502 source : AC5 7) chain B residue 308 type sequence C description BINDING SITE FOR RESIDUE ZN B 2502 source : AC5 8) chain B residue 132 type sequence Y description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 9) chain B residue 177 type sequence Y description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 10) chain B residue 185 type sequence F description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 11) chain B residue 188 type sequence H description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 12) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 13) chain B residue 206 type sequence K description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 14) chain B residue 208 type sequence W description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 15) chain B residue 241 type sequence K description BINDING SITE FOR RESIDUE LEL B 4000 source : AC6 16) chain B residue 105 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1354 source : AC8 17) chain B residue 227 type sequence F description BINDING SITE FOR RESIDUE SO4 B 1354 source : AC9 18) chain B residue 228 type sequence P description BINDING SITE FOR RESIDUE SO4 B 1354 source : AC9 19) chain B residue 229 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1354 source : AC9 20) chain B residue 230 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1354 source : AC9 21) chain B residue 170 type catalytic sequence G description 370 source MCSA : MCSA2 22) chain B residue 177 type catalytic sequence Y description 370 source MCSA : MCSA2 23) chain B residue 188 type catalytic sequence H description 370 source MCSA : MCSA2 24) chain B residue 190 type catalytic sequence E description 370 source MCSA : MCSA2 25) chain B residue 276 type catalytic sequence H description 370 source MCSA : MCSA2 26) chain B residue 288 type catalytic sequence S description 370 source MCSA : MCSA2 27) chain B residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 30) 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 31) 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 32) chain B residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 33) 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 34) 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 35) 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 36) 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 37) chain B residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5

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