eF-site ID 2aw5-ABC PDB Code 2aw5 Chain A, B, C click to enlarge Title Crystal structure of a human malic enzyme Classification OXIDOREDUCTASE Compound NADP-dependent malic enzyme Source Homo sapiens (Human) (MAOX_HUMAN) Sequence A:  GYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQ VLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSIE KFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIAS VLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKLA LYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQRR VRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFRL LNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSDQ TILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLVD SKGLIVKGQEKEKFAHEHEEMKNLEAIVQEIKPTALIGVA AIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQC YKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFPG VALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRLY PPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAFV RSQMYSTDYDQ B:  GYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQ VLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDI EKFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIA SVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKL ALYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQR RVRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFR LLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSD QTILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLV DSKGLIVKGQEKEKFAHEHEEMKNLEAIVQEIKPTALIGV AAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQ CYKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFP GVALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRL YPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAF VRSQMYSTDYDQILPD C:  GYLLTRNPHLNKDLAFTLEERQQLNIHGLLPPSFNSQEIQ VLRVVKNFEHLNSDFDRYLLLMDLQDRNEKLFYRVLTSDI EKFMPIVYTPTVGLACQQYSLVFRKPRGLFITIHDRGHIA SVLNAWPEDVIKAIVVTDGERILGLGDLGCNGMGIPVGKL ALYTACGGMNPQECLPVILDVGTENEELLKDPLYIGLRQR RVRGSEYDDFLDEFMEAVSSKYGMNCLIQFEDFANVNAFR LLNKYRNQYCTFNDDIQGTASVAVAGLLAALRITKNKLSD QTILFQGAGEAALGIAHLIVMALEKEGLPKEKAIKKIWLV DSKGLIVKGQEKEKFAHEHEEMKNLEAIVQEIKPTALIGV AAIGGAFSEQILKDMAAFNERPIIFALSNPTSKAECSAEQ CYKITKGRAIFASGSPFDPVTLPNGQTLYPGQGNNSYVFP GVALGVVACGLRQITDNIFLTTAEVIAQQVSDKHLEEGRL YPPLNTIRDVSLKIAEKIVKDAYQEKTATVYPEPQNKEAF VRSQMYSTDYDQI Description Functional site 1) chain A residue 102 type ACT_SITE sequence Y description Proton donor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 102 type ACT_SITE sequence Y description Proton donor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 102 type ACT_SITE sequence Y description Proton donor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 269 type SITE sequence D description Important for activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 5) chain B residue 269 type SITE sequence D description Important for activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 6) chain C residue 269 type SITE sequence D description Important for activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 7) chain A residue 336 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06801 source Swiss-Prot : SWS_FT_FI6 8) chain B residue 336 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06801 source Swiss-Prot : SWS_FT_FI6 9) chain C residue 336 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06801 source Swiss-Prot : SWS_FT_FI6 10) chain A residue 266-282 type prosite sequence FNDDIQGTASVAVAGLL description MALIC_ENZYMES Malic enzymes signature. FnDDiqGTAsVaVAGLL source prosite : PS00331 11) chain A residue 173 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 173 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI2 13) chain C residue 173 type ACT_SITE sequence K description Proton acceptor => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 155 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 269 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 301 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 408 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 269 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 301 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 408 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 21) chain B residue 155 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 269 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 301 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 408 type BINDING sequence N description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 25) chain C residue 155 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 245 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4 27) chain A residue 246 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 245 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 246 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4 30) chain C residue 245 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4 31) chain C residue 246 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P23368 source Swiss-Prot : SWS_FT_FI4

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