eF-site ID 2yu1-A PDB Code 2yu1 Chain A click to enlarge Title Crystal structure of hJHDM1A complexed with a-ketoglutarate Classification OXIDOREDUCTASE Compound JmjC domain-containing histone demethylation protein 1A Source Homo sapiens (Human) (JHD1A_HUMAN) Sequence A:  RTFDLEEKLHTNKYNANFVTFMEGKDFNVEYIQRGGLRDP LIFKNSDGLGIKMPDPDFTVNDVKMCVGSRRMVDVMDVNT QKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN MVQRPSTVDFIDWVDNMWPRHLKEMQYPKVQKYCLMSVRG CYTDFHVDFGGTSVWYHIHQGGKVFWLIPPTAHNLELYEN WLLSGSQGDIFLGDRVSDCQRIELKQGYTFVIPSGWIHAV YTPTDTLVFGGNFLHSFNIPMQLKIYNIEDRTRVPNKFRY PFYYEMCWYVLERYVYCITNRSHLTKEFQKESLSMDLEQV HLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIAD VKILLEELANSDPKLALTGVPIVQWP Description Functional site 1) chain A residue 212 type sequence H description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 2) chain A residue 214 type sequence D description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 3) chain A residue 284 type sequence H description BINDING SITE FOR RESIDUE FE2 A 600 source : AC1 4) chain A residue 142 type sequence N description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 5) chain A residue 144 type sequence I description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 6) chain A residue 209 type sequence T description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 7) chain A residue 212 type sequence H description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 8) chain A residue 214 type sequence D description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 9) chain A residue 222 type sequence Y description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 10) chain A residue 229 type sequence K description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 11) chain A residue 284 type sequence H description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 12) chain A residue 286 type sequence V description BINDING SITE FOR RESIDUE AKG A 701 source : AC2 13) chain A residue 209 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 229 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 212 type BINDING sequence H description BINDING => ECO:0000305|PubMed:16362057, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 214 type BINDING sequence D description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 284 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00538, ECO:0000269|Ref.27, ECO:0007744|PDB:2YU1, ECO:0007744|PDB:2YU2 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 456 type MOD_RES sequence F description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 460 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 505 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7

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