eF-site ID 3u4s-ABCD PDB Code 3u4s Chain A, B, C, D 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 B:  ETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLA KVVPPKEWKPRASYDDIDDLVIPAPIQQLVTGQSGLFTQY NIQKKAMTVREFRKIANSDKYCTPRYSEFEELERKYWKNL TFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESG ITIEGVNTPYLYFGMWKTSFAWHTEDMDLYSINYLHFGEP KSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRHKMTLI SPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNC AESTNFATRRWIEYGKQAVLCSCRKDMVKISMDVFVRKFQ PERYKLWKAGKDNTVIDHTLPTPEAAEFL C:  ARXSCGGK D:  ARXSCG 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 C residue 9 type sequence X description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 20) chain C residue 11 type sequence C description BINDING SITE FOR RESIDUE 08P A 503 source : AC3 21) chain B residue 188 type sequence H description BINDING SITE FOR RESIDUE NI B 501 source : AC4 22) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE NI B 501 source : AC4 23) chain B residue 276 type sequence H description BINDING SITE FOR RESIDUE NI B 501 source : AC4 24) chain B residue 234 type sequence C description BINDING SITE FOR RESIDUE ZN B 502 source : AC5 25) chain B residue 240 type sequence H description BINDING SITE FOR RESIDUE ZN B 502 source : AC5 26) chain B residue 306 type sequence C description BINDING SITE FOR RESIDUE ZN B 502 source : AC5 27) chain B residue 308 type sequence C description BINDING SITE FOR RESIDUE ZN B 502 source : AC5 28) chain B residue 132 type sequence Y description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 29) chain B residue 177 type sequence Y description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 30) chain B residue 185 type sequence F description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 31) chain B residue 188 type sequence H description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 32) chain B residue 190 type sequence E description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 33) chain B residue 196 type sequence S description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 34) chain B residue 198 type sequence N description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 35) chain B residue 206 type sequence K description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 36) chain B residue 276 type sequence H description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 37) chain B residue 288 type sequence S description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 38) chain D residue 9 type sequence X description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 39) chain D residue 11 type sequence C description BINDING SITE FOR RESIDUE 08P B 503 source : AC6 40) chain A residue 170 type catalytic sequence G description 370 source MCSA : MCSA1 41) chain A residue 177 type catalytic sequence Y description 370 source MCSA : MCSA1 42) chain A residue 188 type catalytic sequence H description 370 source MCSA : MCSA1 43) chain A residue 190 type catalytic sequence E description 370 source MCSA : MCSA1 44) chain A residue 276 type catalytic sequence H description 370 source MCSA : MCSA1 45) chain A residue 288 type catalytic sequence S description 370 source MCSA : MCSA1 46) chain B residue 170 type catalytic sequence G description 370 source MCSA : MCSA2 47) chain B residue 177 type catalytic sequence Y description 370 source MCSA : MCSA2 48) chain B residue 188 type catalytic sequence H description 370 source MCSA : MCSA2 49) chain B residue 190 type catalytic sequence E description 370 source MCSA : MCSA2 50) chain B residue 276 type catalytic sequence H description 370 source MCSA : MCSA2 51) chain B residue 288 type catalytic sequence S description 370 source MCSA : MCSA2 52) chain C residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 53) chain D residue 8 type MOD_RES sequence R description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 54) 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 55) chain B residue 132 type MOD_RES sequence Y description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 198 type MOD_RES sequence N description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 206 type MOD_RES sequence K description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433 source Swiss-Prot : SWS_FT_FI1 58) chain C residue 9 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 9 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 60) chain B residue 188 type MOD_RES sequence H description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 61) chain B residue 276 type MOD_RES sequence H description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 62) chain C residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI3 63) chain D residue 10 type MOD_RES sequence S description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588 source Swiss-Prot : SWS_FT_FI3 64) chain C residue 14 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI5 65) chain C residue 11 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 66) chain D residue 11 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 67) 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 68) 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 69) chain B residue 234 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 70) chain B residue 240 type MOD_RES sequence H 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 71) chain B 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 72) chain B 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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