eF-site ID 1b3o-AB PDB Code 1b3o Chain A, B click to enlarge Title TERNARY COMPLEX OF HUMAN TYPE-II INOSINE MONOPHOSPHATE DEHYDROGENASE WITH 6-CL-IMP AND SELENAZOLE ADENINE DINUCLEOTIDE Classification DEHYDROGENASE Compound PROTEIN (INOSINE MONOPHOSPHATE DEHYDROGENASE 2) Source Homo sapiens (Human) (IMDH2_HUMAN) Sequence A:  TSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQV DLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIG FIHHNCTPEFQANEVRKVKKDYPLASKDAKKQLLCGAAIG THEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIK DKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSRPQA TAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTV MMGSLLAATTEAPGEYDKGSIHKFVPYLIAGIQHSCQDIG AKSLTQVRAMMYSGELKFEKRTSSAQV B:  TSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQV DLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIG FIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRD CGIPITDTGRMGSRLVGIISIMTKREDLVVAPAGITLKEA NEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLAS KDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQ GNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAG VDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRF GVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAP GEYDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYS GELKFEKRTSSAQV Description Functional site 1) chain A residue 68 type sequence S description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 2) chain A residue 322 type sequence R description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 3) chain A residue 327 type sequence S description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 4) chain A residue 364 type sequence D description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 5) chain A residue 366 type sequence G description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 6) chain A residue 385 type sequence M description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 7) chain A residue 387 type sequence G description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 8) chain A residue 388 type sequence S description BINDING SITE FOR RESIDUE CPR A 631 source : AC1 9) chain B residue 68 type sequence S description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 10) chain B residue 322 type sequence R description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 11) chain B residue 328 type sequence G description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 12) chain B residue 329 type sequence S description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 13) chain B residue 331 type sequence C description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 14) chain B residue 334 type sequence Q description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 15) chain B residue 335 type sequence E description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 16) chain B residue 364 type sequence D description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 17) chain B residue 365 type sequence G description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 18) chain B residue 366 type sequence G description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 19) chain B residue 387 type sequence G description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 20) chain B residue 388 type sequence S description BINDING SITE FOR RESIDUE CPR B 631 source : AC2 21) chain A residue 45 type sequence T description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 22) chain A residue 252 type sequence T description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 23) chain A residue 253 type sequence H description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 24) chain A residue 274 type sequence D description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 25) chain A residue 275 type sequence S description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 26) chain A residue 276 type sequence S description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 27) chain A residue 282 type sequence F description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 28) chain A residue 303 type sequence N description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 29) chain A residue 324 type sequence G description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 30) chain A residue 469 type sequence Q description BINDING SITE FOR RESIDUE SAE A 600 source : AC3 31) chain B residue 45 type sequence T description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 32) chain B residue 252 type sequence T description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 33) chain B residue 253 type sequence H description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 34) chain B residue 274 type sequence D description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 35) chain B residue 275 type sequence S description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 36) chain B residue 276 type sequence S description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 37) chain B residue 282 type sequence F description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 38) chain B residue 303 type sequence N description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 39) chain B residue 324 type sequence G description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 40) chain B residue 334 type sequence Q description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 41) chain B residue 466 type sequence H description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 42) chain B residue 469 type sequence Q description BINDING SITE FOR RESIDUE SAE B 601 source : AC4 43) chain B residue 331 type ACT_SITE sequence C description Thioimidate intermediate => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|PubMed:10097070 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 195 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_FI11 45) chain B residue 208 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_FI11 46) chain A residue 274 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 364 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 48) chain A residue 387 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 49) chain B residue 274 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 50) chain B residue 364 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 51) chain B residue 387 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 52) chain A residue 324 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03156 source Swiss-Prot : SWS_FT_FI4 53) chain B residue 324 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03156 source Swiss-Prot : SWS_FT_FI4 54) chain B residue 329 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03156 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 326 type BINDING sequence G description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28 source Swiss-Prot : SWS_FT_FI5 56) chain B residue 326 type BINDING sequence G description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28 source Swiss-Prot : SWS_FT_FI5 57) chain B residue 328 type BINDING sequence G description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 331 type BINDING sequence C description in other chain => ECO:0000255|HAMAP-Rule:MF_03156, ECO:0000269|Ref.28 source Swiss-Prot : SWS_FT_FI5 59) chain B residue 122 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI6 60) chain A residue 400 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8 61) chain B residue 400 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI8

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