eF-site ID 3o6c-A PDB Code 3o6c Chain A click to enlarge Title Pyridoxal phosphate biosynthetic protein PdxJ from Campylobacter jejuni Classification TRANSFERASE Compound Pyridoxine 5'-phosphate synthase Source Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) (PDXJ_CAMJE) Sequence A:  NAXLLGVNIDHIAVLRQARXVNDPDLLEAAFIVARHGDQI TLHVREDRRHAQDFDLENIIKFCKSPVNLECALNDEILNL ALKLKPHRVTLVPEKREELTTEGGLCLNHAKLKQSIEKLQ NANIEVSLFINPSLEDIEKSKILKAQFIELHTGHYANLHN ALFSNISHTAFALKELDQDKKTLQAQFEKELQNLELCAKK GLELGLKVAAGHGLNYKNVKPVVKIKEICELNIGQSIVAR SVFTGLQNAILEXKELIKR Description (1)  Pyridoxine 5'-phosphate synthase (E.C.2.6.99.2) Functional site 1) chain A residue 17 type sequence R description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 2) chain A residue 209 type sequence G description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 3) chain A residue 210 type sequence H description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 4) chain A residue 211 type sequence G description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 5) chain A residue 231 type sequence I description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 6) chain A residue 232 type sequence G description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 7) chain A residue 233 type sequence Q description BINDING SITE FOR RESIDUE PO4 A 301 source : AC1 8) chain A residue 9 type sequence H description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 9) chain A residue 17 type sequence R description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 10) chain A residue 47 type sequence R description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 11) chain A residue 48 type sequence H description BINDING SITE FOR RESIDUE PO4 A 302 source : AC2 12) chain A residue 41 type ACT_SITE sequence H description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 68 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 210 type ACT_SITE sequence H description Proton donor => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 6 type BINDING sequence N description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 8 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 17 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 43 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 48 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 98 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 211 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 232 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 147 type SITE sequence E description Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00279 source Swiss-Prot : SWS_FT_FI4

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