eF-site ID 1dnl-A PDB Code 1dnl Chain A click to enlarge Title X-RAY STRUCTURE OF ESCHERICHIA COLI PYRIDOXINE 5'-PHOSPHATE OXIDASE COMPLEXED WITH FMN AT 1.8 ANGSTROM RESOLUTION Classification OXIDOREDUCTASE Compound PYRIDOXINE 5'-PHOSPHATE OXIDASE Source (PDXH_ECOLI) Sequence A:  GGLRRRDLPADPLTLFERWLSQACEAKLADPTAXVVATVD EHGQPYQRIVLLKHYDEKGXVFYTNLGSRKAHQIENNPRV SLLFPWHTLERQVXVIGKAERLSTLEVXKYFHSRPRDSQI GAWVSKQSSRISARGILESKFLELKQKFQQGEVPLPSFWG GFRVSLEQIEFWQGGEHRLHDRFLYQRENDAWKIDRLAP Description (1)  PYRIDOXINE 5'-PHOSPHATE OXIDASE Functional site 1) chain A residue 23 type sequence R description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 2) chain A residue 24 type sequence R description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 3) chain A residue 120 type sequence R description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 4) chain A residue 152 type sequence A description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 5) chain A residue 153 type sequence R description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 6) chain A residue 215 type sequence R description BINDING SITE FOR RESIDUE PO4 A 275 source : AC1 7) chain A residue 67 type sequence R description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 8) chain A residue 68 type sequence I description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 9) chain A residue 69 type sequence V description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 10) chain A residue 70 type sequence L description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 11) chain A residue 82 type sequence Y description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 12) chain A residue 83 type sequence T description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 13) chain A residue 87 type sequence S description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 14) chain A residue 88 type sequence R description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 15) chain A residue 89 type sequence K description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 16) chain A residue 111 type sequence Q description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 17) chain A residue 146 type sequence Q description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 18) chain A residue 147 type sequence S description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 19) chain A residue 191 type sequence W description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 20) chain A residue 201 type sequence R description BINDING SITE FOR RESIDUE FMN A 250 source : AC2 21) chain A residue 198 type catalytic sequence L description 677 source MCSA : MCSA1 22) chain A residue 192 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 198 type BINDING sequence L description BINDING => ECO:0000269|PubMed:11786019 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 68 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 83 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 89 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 90 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 147 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10903950, ECO:0000269|PubMed:11453690, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11453690 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 130 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11453690 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 134 type BINDING sequence P description BINDING => ECO:0000269|PubMed:11453690 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 138 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11453690 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 112 type BINDING sequence V description BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI3 34) chain A residue 202 type BINDING sequence F description BINDING => ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:15858270 source Swiss-Prot : SWS_FT_FI3 35) chain A residue 188-201 type prosite sequence IEFWQGGEHRLHDR description PYRIDOX_OXIDASE Pyridoxamine 5'-phosphate oxidase signature. IEFWQggehRLHDR source prosite : PS01064

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