eF-site ID 1ohw-AB PDB Code 1ohw Chain A, 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 A:  FDYDGPLMKTEVPGPRSRELMKQLNIIQNAEAVHFFCNYE ESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQ PQNVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQL ITMACGSCSNENAFKTIFMWYRSKERGQSAFSKEELETCM INQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDI PSFDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIV KYRKKKKTVAGIIVEPIQSEGGDNHASDDFFRKLRDISRK HGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKK MMTGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINI IKREDLLSNAAHAGKVLLTGLLDLQARYPQFISRVRGRGT FCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTL VFRDHHAHLFLNIFSDILADF 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 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 B residue 134 type sequence A description BINDING SITE FOR RESIDUE FES A 800 source : AC1 5) chain B residue 135 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 6) chain B residue 138 type sequence C description BINDING SITE FOR RESIDUE FES A 800 source : AC1 7) chain A residue 135 type sequence C description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 8) chain A residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 9) chain A residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 10) chain A residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 11) chain A residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 12) chain A residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 13) chain A residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 14) chain A residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 15) chain A residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 16) chain A residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 17) chain A residue 329 type sequence K description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 18) chain B residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP A 600 source : AC3 19) chain A residue 72 type sequence I description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 20) chain A residue 189 type sequence F description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 21) chain A residue 192 type sequence R description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 22) chain A residue 270 type sequence E description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 23) chain A residue 301 type sequence Q description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 24) chain A residue 329 type sequence K description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 25) chain B residue 351 type sequence F description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 26) chain B residue 352 type sequence N description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 27) chain B residue 353 type sequence T description BINDING SITE FOR RESIDUE VIG A 700 source : AC4 28) chain A residue 353 type sequence T description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 29) chain B residue 135 type sequence C description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 30) chain B residue 136 type sequence G description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 31) chain B residue 137 type sequence S description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 32) chain B residue 140 type sequence N description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 33) chain B residue 189 type sequence F description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 34) chain B residue 190 type sequence H description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 35) chain B residue 191 type sequence G description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 36) chain B residue 265 type sequence E description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 37) chain B residue 298 type sequence D description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 38) chain B residue 300 type sequence V description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 39) chain B residue 301 type sequence Q description BINDING SITE FOR RESIDUE PLP B 600 source : AC5 40) chain A residue 351 type sequence F description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 41) chain A residue 352 type sequence N description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 42) chain A residue 353 type sequence T description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 43) chain B residue 72 type sequence I description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 44) chain B residue 189 type sequence F description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 45) chain B residue 192 type sequence R description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 46) chain B residue 270 type sequence E description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 47) chain B residue 301 type sequence Q description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 48) chain B residue 329 type sequence K description BINDING SITE FOR RESIDUE VIG B 700 source : AC6 49) chain A residue 189 type catalytic sequence F description 854 source MCSA : MCSA1 50) chain A residue 298 type catalytic sequence D description 854 source MCSA : MCSA1 51) chain A residue 329 type catalytic sequence K description 854 source MCSA : MCSA1 52) chain A residue 353 type catalytic sequence T description 854 source MCSA : MCSA1 53) chain B residue 189 type catalytic sequence F description 854 source MCSA : MCSA2 54) chain B residue 298 type catalytic sequence D description 854 source MCSA : MCSA2 55) chain B residue 329 type catalytic sequence K description 854 source MCSA : MCSA2 56) chain B residue 353 type catalytic sequence T description 854 source MCSA : MCSA2 57) chain A residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 135 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 60) chain B residue 138 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 136 type BINDING sequence G description in other chain => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 64) chain B residue 192 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14534310, ECO:0000305|PubMed:10393538 source Swiss-Prot : SWS_FT_FI3 65) chain A residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 66) chain B residue 353 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310 source Swiss-Prot : SWS_FT_FI4 67) chain A residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 68) chain B residue 203 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI5 69) chain A residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 70) chain A residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 71) chain B residue 224 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 72) chain B residue 385 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI6 73) chain A residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 74) chain A residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 75) chain A residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 76) chain A residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 77) chain B residue 251 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 78) chain B residue 290 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 79) chain B residue 424 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 80) chain B residue 442 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P61922 source Swiss-Prot : SWS_FT_FI7 81) 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 82) chain A residue 329 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI8 83) chain B residue 329 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10393538 source Swiss-Prot : SWS_FT_FI8

Display surface Download Links