eF-site ID 2j91-C PDB Code 2j91 Chain C click to enlarge Title Crystal structure of Human Adenylosuccinate Lyase in complex with AMP Classification LYASE Compound ADENYLOSUCCINATE LYASE Source Homo sapiens (Human) (PUR8_HUMAN) Sequence C:  GDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWL WLAEAEQTLGLPITDEQIREMKSNLENIDFKMAAEEEKRL RHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIIL RNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQ LTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGT QASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYT RKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPYKR NPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSAN RRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQE LPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQ EGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQ VQRFLEEEVYPLLKPY Description Functional site 1) chain C residue 111 type sequence T description BINDING SITE FOR RESIDUE CL C1001 source : AC3 2) chain C residue 114 type sequence Y description BINDING SITE FOR RESIDUE CL C1001 source : AC3 3) chain C residue 196 type sequence R description BINDING SITE FOR RESIDUE CL C1001 source : AC3 4) chain C residue 199 type sequence K description BINDING SITE FOR RESIDUE CL C1001 source : AC3 5) chain C residue 200 type sequence G description BINDING SITE FOR RESIDUE CL C1001 source : AC3 6) chain C residue 159 type sequence H description BINDING SITE FOR RESIDUE AMP A1000 source : AC5 7) chain C residue 85 type sequence R description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 8) chain C residue 86 type sequence H description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 9) chain C residue 87 type sequence D description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 10) chain C residue 112 type sequence S description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 11) chain C residue 241 type sequence Q description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 12) chain C residue 329 type sequence R description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 13) chain C residue 331 type sequence L description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 14) chain C residue 334 type sequence S description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 15) chain C residue 335 type sequence A description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 16) chain C residue 338 type sequence R description BINDING SITE FOR RESIDUE AMP B1000 source : AC6 17) chain C residue 20 type sequence R description BINDING SITE FOR RESIDUE AMP C1000 source : AC7 18) chain C residue 21 type sequence Y description BINDING SITE FOR RESIDUE AMP C1000 source : AC7 19) chain C residue 299 type sequence M description BINDING SITE FOR RESIDUE AMP C1000 source : AC7 20) chain C residue 303 type sequence R description BINDING SITE FOR RESIDUE AMP C1000 source : AC7 21) chain C residue 35 type sequence K description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 22) chain C residue 39 type sequence W description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 23) chain C residue 87 type sequence D description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 24) chain C residue 116 type sequence G description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 25) chain C residue 120 type sequence D description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 26) chain C residue 334 type sequence S description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 27) chain C residue 338 type sequence R description BINDING SITE FOR RESIDUE GOL C1473 source : BC2 28) chain C residue 159 type ACT_SITE sequence H description Proton donor/acceptor => ECO:0000269|PubMed:22812634 source Swiss-Prot : SWS_FT_FI1 29) chain C residue 20 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 30) chain C residue 303 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 31) chain C residue 85 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 32) chain C residue 111 type BINDING sequence T description in other chain source Swiss-Prot : SWS_FT_FI3 33) chain C residue 241 type BINDING sequence Q description in other chain source Swiss-Prot : SWS_FT_FI3 34) chain C residue 329 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 35) chain C residue 334 type BINDING sequence S description in other chain source Swiss-Prot : SWS_FT_FI3 36) chain C residue 338 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI3 37) chain C residue 147 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 38) chain C residue 295 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 39) chain C residue 415 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI6

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