eF-site ID 1i1k-ABC PDB Code 1i1k Chain A, B, C click to enlarge Title CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. Classification TRANSFERASE Compound BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE Source (ILVE_ECOLI) Sequence A:  KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYD SHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACR DVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAA FPWALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLV GSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTP PFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLAD EVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFG LFTGETEDKWGWLDQVNQ B:  KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYD SHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACR DVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAA FPWALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLV GSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTP PFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLAD EVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFG LFTGETEDKWGWLDQVNQ C:  KADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYD SHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACR DVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAA FPWALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLV GSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTP PFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLAD EVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFG LFTGETEDKWGWLDQVNQ Description (1)  AMINOTRANSFERASE(E.C.2.6.1.42), PYRIDOXAL-5'-PHOSPHATE Functional site 1) chain A residue 59 type sequence R description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 2) chain A residue 159 type sequence K description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 3) chain A residue 164 type sequence Y description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 4) chain A residue 193 type sequence E description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 5) chain A residue 196 type sequence G description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 6) chain A residue 197 type sequence E description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 7) chain A residue 217 type sequence L description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 8) chain A residue 219 type sequence G description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 9) chain A residue 220 type sequence I description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 10) chain A residue 221 type sequence T description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 11) chain A residue 257 type sequence T description BINDING SITE FOR RESIDUE PLP A 413 source : AC1 12) chain B residue 559 type sequence R description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 13) chain B residue 648 type sequence R description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 14) chain B residue 659 type sequence K description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 15) chain B residue 664 type sequence Y description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 16) chain B residue 693 type sequence E description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 17) chain B residue 696 type sequence G description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 18) chain B residue 697 type sequence E description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 19) chain B residue 698 type sequence N description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 20) chain B residue 717 type sequence L description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 21) chain B residue 719 type sequence G description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 22) chain B residue 720 type sequence I description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 23) chain B residue 721 type sequence T description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 24) chain B residue 757 type sequence T description BINDING SITE FOR RESIDUE PLP B 913 source : AC2 25) chain C residue 1059 type sequence R description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 26) chain C residue 1159 type sequence K description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 27) chain C residue 1164 type sequence Y description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 28) chain C residue 1193 type sequence E description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 29) chain C residue 1196 type sequence G description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 30) chain C residue 1197 type sequence E description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 31) chain C residue 1217 type sequence L description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 32) chain C residue 1219 type sequence G description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 33) chain C residue 1220 type sequence I description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 34) chain C residue 1221 type sequence T description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 35) chain C residue 1257 type sequence T description BINDING SITE FOR RESIDUE PLP C 1413 source : AC3 36) chain A residue 159 type catalytic sequence K description 813 source MCSA : MCSA1 37) chain B residue 659 type catalytic sequence K description 813 source MCSA : MCSA2 38) chain C residue 1159 type catalytic sequence K description 813 source MCSA : MCSA3 39) chain A residue 193-222 type prosite sequence EGAGENLFEVKDGVLFTPPFTSSALPGITR description AA_TRANSFER_CLASS_4 Aminotransferases class-IV signature. EgAgeNLFevkdgv......LfTppftssa.LpGItR source prosite : PS00770 40) chain A residue 159 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1 41) chain B residue 659 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1 42) chain C residue 1159 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI1

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