eF-site ID 1ohw-B PDB Code 1ohw Chain B 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 B:  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 B residue 134 type sequence A description BINDING SITE FOR RESIDUE FES A 800 source : AC1 2) chain B residue 135 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 3) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 4) chain B residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 5) chain B residue 351 type sequence F description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 6) chain B residue 352 type sequence N description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 7) chain B residue 353 type sequence T description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 8) chain B residue 135 type sequence C description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 9) chain B residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 10) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 11) chain B residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 12) chain B residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 13) chain B residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 14) chain B residue 191 type sequence G description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 15) chain B residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 16) chain B residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 17) chain B residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 18) chain B residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 19) chain B residue 72 type sequence I description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 20) chain B residue 189 type sequence F description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 21) chain B residue 192 type sequence R description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 22) chain B residue 270 type sequence E description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 23) chain B residue 301 type sequence Q description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 24) chain B residue 329 type sequence K description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 25) chain B residue 189 type catalytic sequence F description 854 source MCSA : MCSA2 26) chain B residue 298 type catalytic sequence D description 854 source MCSA : MCSA2 27) chain B residue 329 type catalytic sequence K description 854 source MCSA : MCSA2 28) chain B residue 353 type catalytic sequence T description 854 source MCSA : MCSA2 29) chain B residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 33) chain B residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 34) chain B residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 35) chain B residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 36) chain B residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 37) chain B residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 38) chain B residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 39) chain B residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 40) chain B residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 41) chain B 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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