eF-site ID 6h4o-C PDB Code 6h4o Chain C click to enlarge Title Crystal structure of human KDM4A in complex with compound 18a Classification OXIDOREDUCTASE Compound Lysine-specific demethylase 4A Source (KDM4A_HUMAN) Sequence C:  SARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPP KEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNIQKK AMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTFNPP IYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEG VNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKSWYS VPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISPLML KKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTN FATRRWIEYGKQAVLCSCMVKISMDVFVRKFQPERYKLWK AGKDNTVIDHTLPTPEAAEFL Description Functional site 1) chain C residue 75 type sequence V description binding site for residue GOL A 404 source : AC4 2) chain C residue 76 type sequence T description binding site for residue GOL A 404 source : AC4 3) chain C residue 77 type sequence G description binding site for residue GOL A 404 source : AC4 4) chain C residue 126 type sequence T description binding site for residue GOL A 404 source : AC4 5) chain C residue 127 type sequence F description binding site for residue GOL A 404 source : AC4 6) chain C residue 188 type sequence H description binding site for residue ZN C 401 source : AD1 7) chain C residue 190 type sequence E description binding site for residue ZN C 401 source : AD1 8) chain C residue 276 type sequence H description binding site for residue ZN C 401 source : AD1 9) chain C residue 234 type sequence C description binding site for residue ZN C 402 source : AD2 10) chain C residue 240 type sequence H description binding site for residue ZN C 402 source : AD2 11) chain C residue 306 type sequence C description binding site for residue ZN C 402 source : AD2 12) chain C residue 308 type sequence C description binding site for residue ZN C 402 source : AD2 13) chain C residue 132 type sequence Y description binding site for residue FQH C 403 source : AD3 14) chain C residue 135 type sequence D description binding site for residue FQH C 403 source : AD3 15) chain C residue 169 type sequence E description binding site for residue FQH C 403 source : AD3 16) chain C residue 175 type sequence Y description binding site for residue FQH C 403 source : AD3 17) chain C residue 177 type sequence Y description binding site for residue FQH C 403 source : AD3 18) chain C residue 185 type sequence F description binding site for residue FQH C 403 source : AD3 19) chain C residue 188 type sequence H description binding site for residue FQH C 403 source : AD3 20) chain C residue 190 type sequence E description binding site for residue FQH C 403 source : AD3 21) chain C residue 191 type sequence D description binding site for residue FQH C 403 source : AD3 22) chain C residue 206 type sequence K description binding site for residue FQH C 403 source : AD3 23) chain C residue 208 type sequence W description binding site for residue FQH C 403 source : AD3 24) chain C residue 276 type sequence H description binding site for residue FQH C 403 source : AD3 25) chain C residue 12 type sequence A description binding site for residue DMS C 404 source : AD4 26) chain C residue 13 type sequence R description binding site for residue DMS C 404 source : AD4 27) chain C residue 257 type sequence F description binding site for residue DMS C 404 source : AD4 28) chain C residue 294 type sequence R description binding site for residue DMS C 405 source : AD5 29) chain C residue 324 type sequence F description binding site for residue DMS C 405 source : AD5 30) chain C residue 132 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 31) chain C residue 198 type BINDING sequence N description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 206 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16677698 source Swiss-Prot : SWS_FT_FI1 33) 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 34) 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 35) chain C residue 190 type BINDING sequence E description BINDING => ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168 source Swiss-Prot : SWS_FT_FI3 36) 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 37) 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 38) 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 39) 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 40) chain C residue 170 type catalytic sequence G description 370 source MCSA : MCSA3 41) chain C residue 177 type catalytic sequence Y description 370 source MCSA : MCSA3 42) chain C residue 188 type catalytic sequence H description 370 source MCSA : MCSA3 43) chain C residue 190 type catalytic sequence E description 370 source MCSA : MCSA3 44) chain C residue 276 type catalytic sequence H description 370 source MCSA : MCSA3 45) chain C residue 288 type catalytic sequence S description 370 source MCSA : MCSA3 46) chain C residue 241 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:B2RXH2 source Swiss-Prot : SWS_FT_FI5

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