eF-site ID 2oat-ABC PDB Code 2oat Chain A, B, C click to enlarge Title ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE 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 55 type sequence Y description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 2) chain A residue 141 type sequence T description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 3) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 4) chain A residue 143 type sequence V description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 5) chain A residue 177 type sequence F description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 6) chain A residue 178 type sequence W description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 7) chain A residue 180 type sequence R description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 8) chain A residue 230 type sequence E description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 9) chain A residue 235 type sequence E description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 10) chain A residue 263 type sequence D description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 11) chain A residue 266 type sequence Q description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 12) chain A residue 292 type sequence K description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 13) chain B residue 320 type sequence G description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 14) chain B residue 321 type sequence S description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 15) chain B residue 322 type sequence T description BINDING SITE FOR RESIDUE PFM A 440 source : AC1 16) chain A residue 320 type sequence G description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 17) chain A residue 321 type sequence S description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 18) chain A residue 322 type sequence T description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 19) chain B residue 55 type sequence Y description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 20) chain B residue 85 type sequence Y description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 21) chain B residue 141 type sequence T description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 22) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 23) chain B residue 143 type sequence V description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 24) chain B residue 177 type sequence F description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 25) chain B residue 178 type sequence W description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 26) chain B residue 180 type sequence R description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 27) chain B residue 230 type sequence E description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 28) chain B residue 263 type sequence D description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 29) chain B residue 265 type sequence I description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 30) chain B residue 266 type sequence Q description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 31) chain B residue 292 type sequence K description BINDING SITE FOR RESIDUE PFM B 440 source : AC2 32) chain C residue 55 type sequence Y description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 33) chain C residue 85 type sequence Y description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 34) chain C residue 141 type sequence T description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 35) chain C residue 142 type sequence G description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 36) chain C residue 143 type sequence V description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 37) chain C residue 177 type sequence F description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 38) chain C residue 178 type sequence W description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 39) chain C residue 180 type sequence R description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 40) chain C residue 230 type sequence E description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 41) chain C residue 263 type sequence D description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 42) chain C residue 265 type sequence I description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 43) chain C residue 266 type sequence Q description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 44) chain C residue 292 type sequence K description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 45) chain C residue 320 type sequence G description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 46) chain C residue 321 type sequence S description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 47) chain C residue 322 type sequence T description BINDING SITE FOR RESIDUE PFM C 440 source : AC3 48) chain A residue 177 type catalytic sequence F description 929 source MCSA : MCSA1 49) chain A residue 263 type catalytic sequence D description 929 source MCSA : MCSA1 50) chain A residue 292 type catalytic sequence K description 929 source MCSA : MCSA1 51) chain B residue 177 type catalytic sequence F description 929 source MCSA : MCSA2 52) chain B residue 263 type catalytic sequence D description 929 source MCSA : MCSA2 53) chain B residue 292 type catalytic sequence K description 929 source MCSA : MCSA2 54) chain C residue 177 type catalytic sequence F description 929 source MCSA : MCSA3 55) chain C residue 263 type catalytic sequence D description 929 source MCSA : MCSA3 56) chain C residue 292 type catalytic sequence K description 929 source MCSA : MCSA3 57) 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 58) chain A residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 60) chain C residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 61) chain C residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 62) chain C residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 63) chain C residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 64) chain C residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 68) chain A residue 421 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 49 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 66 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 386 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 72) chain B residue 392 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI1 73) chain A residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 74) chain B residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 75) chain C residue 102 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 77) chain A residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 78) chain A residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 79) chain B residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 80) chain B residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 81) chain B residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 82) chain C residue 107 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 83) chain C residue 362 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 84) chain C residue 405 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758 source Swiss-Prot : SWS_FT_FI3 85) chain A residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4 86) chain B residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4 87) chain C residue 292 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226 source Swiss-Prot : SWS_FT_FI4

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