eF-site ID 1ohw-A PDB Code 1ohw Chain A click to enlarge Title 4-AMINOBUTYRATE-AMINOTRANSFERASE inactivated by gamma-vinyl GABA Classification TRANSFERASE Compound 4-AMINOBUTYRATE AMINOTRANSFERASE Source ORGANISM_COMMON: PIG; ORGANISM_SCIENTIFIC: SUS SCROFA; Sequence A:  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 A residue 134 type sequence A description BINDING SITE FOR RESIDUE FES A 800 source : AC1 2) chain A residue 135 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 3) chain A residue 138 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 4) chain A residue 135 type sequence C description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 5) chain A residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 6) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 7) chain A residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 8) chain A residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 9) chain A residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 10) chain A residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 11) chain A residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 12) chain A residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 13) chain A residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 14) chain A residue 329 type sequence K description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 15) chain A residue 72 type sequence I description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 16) chain A residue 189 type sequence F description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 17) chain A residue 192 type sequence R description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 18) chain A residue 270 type sequence E description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 19) chain A residue 301 type sequence Q description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 20) chain A residue 329 type sequence K description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 21) chain A residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 22) chain A residue 351 type sequence F description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 23) chain A residue 352 type sequence N description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 24) chain A residue 353 type sequence T description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 25) chain A residue 189 type catalytic sequence F description 854 source MCSA : MCSA1 26) chain A residue 298 type catalytic sequence D description 854 source MCSA : MCSA1 27) chain A residue 329 type catalytic sequence K description 854 source MCSA : MCSA1 28) chain A residue 353 type catalytic sequence T description 854 source MCSA : MCSA1 29) chain A residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 33) chain A residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 34) chain A residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 35) chain A residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 38) chain A residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 39) chain A residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 40) chain A residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 41) chain A residue 295-334 type prosite sequence FLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKKMMTG description AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FLvDEVqtgGG.StGkfwahehwglddpa..DVMtfSKkmmTG source prosite : PS00600 42) chain A 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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