eF-site ID 1bjn-AB PDB Code 1bjn Chain A, B click to enlarge Title STRUCTURE OF PHOSPHOSERINE AMINOTRANSFERASE FROM ESCHERICHIA COLI Classification AMINOTRANSFERASE Compound PHOSPHOSERINE AMINOTRANSFERASE Source Escherichia coli (strain K12) (SERC_ECOLI) Sequence A:  QIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHR GKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAA VPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAK VTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDET PDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQXNIGP AGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPP TFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDN SDFYRNDVAKRNRSRMNVPFQLADSALDKLFLEESFAAGL HALKGHRVVGGMRASIYNAMPLEGVKALTDFMVEFERRHG B:  QIFNFSSGPAMLPAEVLKQAQQELRDWNGLGTSVMEVSHR GKEFIQVAEEAEKDFRDLLNVPSNYKVLFCHGGGRGQFAA VPLNILGDKTTADYVDAGYWAASAIKEAKKYCTPNVFDAK VTVDGLRAVKPMREWQLSDNAAYMHYCPNETIDGIAIDET PDFGADVVVAADFSSTILSRPIDVSRYGVIYAGAQXNIGP AGLTIVIVREDLLGKANIACPSILDYSILNDNGSMFNTPP TFAWYLSGLVFKWLKANGGVAEMDKINQQKAELLYGVIDN SDFYRNDVAKRNRSRMNVPFQLADSALDKLFLEESFAAGL HALKGHRVVGGMRASIYNAMPLEGVKALTDFMVEFERRHG Description (1)  PHOSPHOSERINE AMINOTRANSFERASE Functional site 1) chain A residue 198 type sequence X description PLP BINDING RESIDUE, MOLECULE A. source : PPA 2) chain B residue 198 type sequence X description PLP BINDING RESIDUE, MOLECULE B. source : PPB 3) chain A residue 102 type catalytic sequence W description 424 source MCSA : MCSA1 4) chain A residue 174 type catalytic sequence D description 424 source MCSA : MCSA1 5) chain A residue 198 type catalytic sequence X description 424 source MCSA : MCSA1 6) chain B residue 102 type catalytic sequence W description 424 source MCSA : MCSA2 7) chain B residue 174 type catalytic sequence D description 424 source MCSA : MCSA2 8) chain B residue 198 type catalytic sequence X description 424 source MCSA : MCSA2 9) chain A residue 189-208 type prosite sequence YGVIYAGAQXNIGPAGLTIV description AA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. YGVIyaGAQKnigpa.GlTiV source prosite : PS00595 10) chain A residue 9 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI1 11) chain B residue 42 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 12) chain B residue 76 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 13) chain B residue 102 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 14) chain B residue 153 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 15) chain B residue 174 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 16) chain B residue 197 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 17) chain B residue 239 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 18) chain A residue 42 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI1 19) chain A residue 76 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI1 20) chain A residue 102 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI1 21) chain A residue 153 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI1 22) chain A residue 174 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 23) chain A residue 197 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI1 24) chain A residue 239 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI1 25) chain B residue 9 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI1 26) chain A residue 198 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2 27) chain B residue 198 type MOD_RES sequence X description N6-(pyridoxal phosphate)lysine source Swiss-Prot : SWS_FT_FI2

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