eF-site ID 1oat-ABC PDB Code 1oat Chain A, B, C click to enlarge Title ORNITHINE AMINOTRANSFERASE Classification AMINOTRANSFERASE Compound ORNITHINE AMINOTRANSFERASE Source Homo sapiens (Human) (OAT_HUMAN) Sequence A:  GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEG RKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAF YNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARK WGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYD GFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRW LAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIK PGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGII LRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCL RLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT ILSF B:  GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEG RKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAF YNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARK WGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYD GFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRW LAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIK PGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGII LRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCL RLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT ILSF C:  GPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEG RKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAF YNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARK WGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYD GFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGE AGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRW LAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIK PGEHGSTYGGNPLGCRVAIAALEVLEEENLAENADKLGII LRNELMKLPSDVVTAVRGKGLLNAIVIKETKDWDAWKVCL RLRDNGLLAKPTHGDIIRFAPPLVIKEDELRESIEIINKT ILSF Description Functional site 1) chain A residue 177 type catalytic sequence F description 929 source MCSA : MCSA1 2) chain A residue 263 type catalytic sequence D description 929 source MCSA : MCSA1 3) chain A residue 292 type catalytic sequence K description 929 source MCSA : MCSA1 4) chain B residue 177 type catalytic sequence F description 929 source MCSA : MCSA2 5) chain B residue 263 type catalytic sequence D description 929 source MCSA : MCSA2 6) chain B residue 292 type catalytic sequence K description 929 source MCSA : MCSA2 7) chain C residue 177 type catalytic sequence F description 929 source MCSA : MCSA3 8) chain C residue 263 type catalytic sequence D description 929 source MCSA : MCSA3 9) chain C residue 292 type catalytic sequence K description 929 source MCSA : MCSA3 10) chain A residue 260-297 type prosite sequence FIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEIqt.GLaRtGrwlavdyenvrp....DIVllGKalsGG source prosite : PS00600 11) chain A residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 12) chain B residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 13) chain C residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 28) chain C residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 30) chain A residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 31) chain A residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 32) chain B residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 34) chain B residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 35) chain C residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 36) chain C residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 37) chain C residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 38) chain A residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4 39) chain B residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4 40) chain C residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4

Display surface Download Links