eF-site ID 1ohy-CD PDB Code 1ohy Chain C, D click to enlarge Title 4-AMINOBUTYRATE-AMINOTRANSFERASE inactivated by gamma-ethynyl GABA Classification TRANSFERASE Compound 4-AMINOBUTYRATE AMINOTRANSFERASE Source ORGANISM_COMMON: PIG; ORGANISM_SCIENTIFIC: SUS SCROFA; Sequence C:  FDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYE ESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQ PQNVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQL ITMACGSCSNENAFKTIFMWYRSKERGQSAFSKEELETCM INQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDI PSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIV KYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDISRK HGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKK MMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINI IKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRGT FCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTL VFRDHHAHLFLNIFSDILADF D:  FDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYE ESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQ PQNVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQL ITMACGSCSNENAFKTIFMWYRSKERGQSAFSKEELETCM INQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDI PSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIV KYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDISRK HGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKK MMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINI IKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRGT FCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTL VFRDHHAHLFLNIFSDILADF Description (1)  4-AMINOBUTYRATE AMINOTRANSFERASE (E.C.2.6.1.19) Functional site 1) chain C residue 134 type sequence A description BINDING SITE FOR RESIDUE FES C 800 source : AC2 2) chain C residue 135 type sequence C description BINDING SITE FOR RESIDUE FES C 800 source : AC2 3) chain C residue 138 type sequence C description BINDING SITE FOR RESIDUE FES C 800 source : AC2 4) chain D residue 134 type sequence A description BINDING SITE FOR RESIDUE FES C 800 source : AC2 5) chain D residue 135 type sequence C description BINDING SITE FOR RESIDUE FES C 800 source : AC2 6) chain D residue 138 type sequence C description BINDING SITE FOR RESIDUE FES C 800 source : AC2 7) chain C residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 8) chain C residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 9) chain C residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 10) chain C residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 11) chain C residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 12) chain C residue 191 type sequence G description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 13) chain C residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 14) chain C residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 15) chain C residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 16) chain C residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 17) chain C residue 329 type sequence K description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 18) chain D residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP C 600 source : AC7 19) chain C residue 72 type sequence I description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 20) chain C residue 189 type sequence F description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 21) chain C residue 192 type sequence R description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 22) chain C residue 329 type sequence K description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 23) chain D residue 351 type sequence F description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 24) chain D residue 353 type sequence T description BINDING SITE FOR RESIDUE GEG C 700 source : AC8 25) chain C residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 26) chain D residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 27) chain D residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 28) chain D residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 29) chain D residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 30) chain D residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 31) chain D residue 191 type sequence G description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 32) chain D residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 33) chain D residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 34) chain D residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 35) chain D residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 36) chain D residue 329 type sequence K description BINDING SITE FOR RESIDUE PLP D 600 source : AC9 37) chain C residue 351 type sequence F description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 38) chain C residue 353 type sequence T description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 39) chain D residue 72 type sequence I description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 40) chain D residue 189 type sequence F description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 41) chain D residue 192 type sequence R description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 42) chain D residue 270 type sequence E description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 43) chain D residue 329 type sequence K description BINDING SITE FOR RESIDUE GEG D 700 source : BC1 44) chain C residue 189 type catalytic sequence F description 854 source MCSA : MCSA3 45) chain C residue 298 type catalytic sequence D description 854 source MCSA : MCSA3 46) chain C residue 329 type catalytic sequence K description 854 source MCSA : MCSA3 47) chain C residue 353 type catalytic sequence T description 854 source MCSA : MCSA3 48) chain D residue 189 type catalytic sequence F description 854 source MCSA : MCSA4 49) chain D residue 298 type catalytic sequence D description 854 source MCSA : MCSA4 50) chain D residue 329 type catalytic sequence K description 854 source MCSA : MCSA4 51) chain D residue 353 type catalytic sequence T description 854 source MCSA : MCSA4 52) chain C residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 53) chain C residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 54) chain D residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 55) chain D residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 56) chain C residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 57) chain D residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 59) chain D residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 60) chain C residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 61) chain D residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 62) chain C residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 63) chain D residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 64) chain C residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 65) chain C residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 66) chain D residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 67) chain D residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 68) chain C residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 69) chain C residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 70) chain C residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 71) chain D residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 72) chain D residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 73) chain D residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 74) chain D residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 75) chain C residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 76) chain C residue 329 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI8 77) chain D residue 329 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI8

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