eF-site ID 6taj-.AAA.BBB PDB Code 6taj Chain AAA, BBB click to enlarge Title Crystal structure of Escherichia coli Orotate Phosphoribosyltransferase in complex with Orotic acid 1.60 Angstrom resolution Classification TRANSFERASE Compound Orotate phosphoribosyltransferase Source (PYRE_ECOLI) Sequence AAA:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT TAVALAEHHDLDLPYCFNRKEGNLVGSALQGRVMLVDDVI TAGTAIRESMEIIQANGATLAGVLISLDRQERGRGEISAI QEVERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAY REEFGV BBB:  MKPYQRQFIEFALSKQVLKFGEFTLKSGRKSPYFFNAGLF NTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATT TAVALAEHHDLDLPYCFNRNLVGSALQGRVMLVDDVITAG TAIRESMEIIQANGATLAGVLISLDRQERGRGEISAIQEV ERDYNCKVISIITLKDLIAYLEEKPEMAEHLAAVKAYREE FGV Description Functional site 1) chain AAA residue 120-132 type prosite sequence VMLVDDVITAGTA description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VMLVDDVITAGtA source prosite : PS00103 2) chain AAA residue 26 type BINDING sequence K description in other chain => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI1 3) chain AAA residue 124 type BINDING sequence D description in other chain => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI1 4) chain BBB residue 26 type BINDING sequence K description in other chain => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI1 5) chain BBB residue 124 type BINDING sequence D description in other chain => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI1 6) chain AAA residue 34 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 7) chain AAA residue 128 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 8) chain AAA residue 156 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 9) chain BBB residue 34 type BINDING sequence F description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 10) chain BBB residue 128 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 11) chain BBB residue 156 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01208 source Swiss-Prot : SWS_FT_FI2 12) chain AAA residue 72 type BINDING sequence Y description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002 source Swiss-Prot : SWS_FT_FI3 13) chain AAA residue 100 type BINDING sequence K description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002 source Swiss-Prot : SWS_FT_FI3 14) chain BBB residue 72 type BINDING sequence Y description in other chain => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002 source Swiss-Prot : SWS_FT_FI3 15) chain AAA residue 99 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002 source Swiss-Prot : SWS_FT_FI4 16) chain BBB residue 99 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000305|PubMed:8620002 source Swiss-Prot : SWS_FT_FI4

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