eF-site ID 6avs-A PDB Code 6avs Chain A click to enlarge Title Complex structure of JMJD5 and Symmetric Monomethyl-Arginine (MMA) Classification OXIDOREDUCTASE Compound Lysine-specific demethylase 8 Source Homo sapiens (Human) (KDM8_HUMAN) Sequence A:  GGTVPRLHRPSLQHFREQFLVPGRPVILKGVADHWPCMQK WSLEYIQEIAGCRTVPVEVGSRYTDEEWSQTLMTVNEFIS KYIVNEPRDVGYLAQHQLFDQIPELKQDISIPDYCSLGDG EEEEITINAWFGPQGTISPLHQDPQQNFLVQVMGRKYIRL YSPQESGALYPHDTHLLHNTSQVDVENPDLEKFPKFAKAP FLSCILSPGEILFIPVKYWHYVRALDLSFSVSFWWS Description Functional site 1) chain A residue 321 type sequence H description binding site for residue ZN A 501 source : AC1 2) chain A residue 323 type sequence D description binding site for residue ZN A 501 source : AC1 3) chain A residue 400 type sequence H description binding site for residue ZN A 501 source : AC1 4) chain A residue 238 type sequence E description binding site for residue NMM A 502 source : AC2 5) chain A residue 243 type sequence Y description binding site for residue NMM A 502 source : AC2 6) chain A residue 272 type sequence Y description binding site for residue NMM A 502 source : AC2 7) chain A residue 275 type sequence Q description binding site for residue NMM A 502 source : AC2 8) chain A residue 310 type sequence W description binding site for residue NMM A 502 source : AC2 9) chain A residue 318 type sequence S description binding site for residue NMM A 502 source : AC2 10) chain A residue 321 type sequence H description binding site for residue NMM A 502 source : AC2 11) chain A residue 323 type sequence D description binding site for residue NMM A 502 source : AC2 12) chain A residue 289 type BINDING sequence I description BINDING => ECO:0000269|PubMed:22851697, ECO:0000269|PubMed:29459673, ECO:0000269|PubMed:29563586, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:3UYJ, ECO:0007744|PDB:4GJZ, ECO:0007744|PDB:4QU1, ECO:0007744|PDB:5FBJ source Swiss-Prot : SWS_FT_FI2 13) chain A residue 298 type BINDING sequence G description BINDING => ECO:0000269|PubMed:22851697, ECO:0000269|PubMed:29459673, ECO:0000269|PubMed:29563586, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:3UYJ, ECO:0007744|PDB:4GJZ, ECO:0007744|PDB:4QU1, ECO:0007744|PDB:5FBJ source Swiss-Prot : SWS_FT_FI2 14) chain A residue 234 type BINDING sequence T description BINDING => ECO:0000269|PubMed:22851697, ECO:0000269|PubMed:29459673, ECO:0000269|PubMed:29563586, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:3UYJ, ECO:0007744|PDB:4GJZ, ECO:0007744|PDB:4QU1, ECO:0007744|PDB:5FBJ source Swiss-Prot : SWS_FT_FI2 15) chain A residue 376 type BINDING sequence F description BINDING => ECO:0000269|PubMed:22851697, ECO:0000269|PubMed:29459673, ECO:0000269|PubMed:29563586, ECO:0007744|PDB:3UYJ, ECO:0007744|PDB:4GJZ source Swiss-Prot : SWS_FT_FI4 16) chain A residue 200 type BINDING sequence L description BINDING => ECO:0000269|PubMed:29459673 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 237 type BINDING sequence V description BINDING => ECO:0000269|PubMed:29459673 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 280 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459673 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 283 type BINDING sequence P description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000305|PubMed:22851697, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:4GJY, ECO:0007744|PDB:4GJZ source Swiss-Prot : SWS_FT_FI3 20) chain A residue 285 type BINDING sequence L description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000305|PubMed:22851697, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:4GJY, ECO:0007744|PDB:4GJZ source Swiss-Prot : SWS_FT_FI3 21) chain A residue 362 type BINDING sequence Q description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000305|PubMed:22851697, ECO:0000305|PubMed:24100311, ECO:0007744|PDB:4GJY, ECO:0007744|PDB:4GJZ source Swiss-Prot : SWS_FT_FI3

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