eF-site ID 3u4s-A PDB Code 3u4s Chain A click to enlarge Title Histone Lysine demethylase JMJD2A in complex with T11C peptide substrate crosslinked to N-oxalyl-D-cysteine Classification OXIDOREDUCTASE/OXIDOREDUCTASE SUBSTRATE Compound Lysine-specific demethylase 4A Source Homo sapiens (Human) (H31_HUMAN) Sequence A:  LNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKV VPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQYNI QKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNLTF NPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGIT IEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEPKS WYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLISP LMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAE STNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQPE RYKLWKAGKDNTVIDHTLPTPEAAE Description Functional site 1) chain A residue 188 type sequence H description BINDING SITE FOR RESIDUE NI A 501 source : AC1 2) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE NI A 501 source : AC1 3) chain A residue 276 type sequence H description BINDING SITE FOR RESIDUE NI A 501 source : AC1 4) chain A residue 234 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 5) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 6) chain A residue 306 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 7) chain A residue 308 type sequence C description BINDING SITE FOR RESIDUE ZN A 502 source : AC2 8) chain A residue 132 type sequence Y description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 9) chain A residue 177 type sequence Y description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 10) chain A residue 185 type sequence F description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 11) chain A residue 188 type sequence H description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 12) chain A residue 190 type sequence E description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 13) chain A residue 196 type sequence S description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 14) chain A residue 198 type sequence N description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 15) chain A residue 206 type sequence K description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 16) chain A residue 208 type sequence W description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 17) chain A residue 276 type sequence H description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 18) chain A residue 288 type sequence S description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 19) chain A residue 170 type catalytic sequence G description 370 source MCSA : MCSA1 20) chain A residue 177 type catalytic sequence Y description 370 source MCSA : MCSA1 21) chain A residue 188 type catalytic sequence H description 370 source MCSA : MCSA1 22) chain A residue 190 type catalytic sequence E description 370 source MCSA : MCSA1 23) chain A residue 276 type catalytic sequence H description 370 source MCSA : MCSA1 24) chain A residue 288 type catalytic sequence S description 370 source MCSA : MCSA1 25) chain A residue 206 type MOD_RES sequence K description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 306 type MOD_RES sequence C description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 308 type MOD_RES sequence C description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803 source Swiss-Prot : SWS_FT_FI4

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