eF-site ID 2g6v-AB PDB Code 2g6v Chain A, B click to enlarge Title The crystal structure of ribD from Escherichia coli Classification HYDROLASE, OXIDOREDUCTASE Compound Riboflavin biosynthesis protein ribD Source Escherichia coli (strain K12) (RIBD_ECOLI) Sequence A:  TLYIQGQDEYYXARALKLAQRGRFTTHPNPNVGCVIVKDG EIVGEGYHQRAGEPHAEVHALRXAGEKAKGATAYVTLEPC PCCDALIAAGVARVVASXQDPNPQVAGRGLYRLQQAGIDV SHGLXXSEAEQLNKGFLKRXRTGFPYIQLKLGASLDGRTA XESQWITSPQARRDVQLLRAQSHAILTSSATVLADDPALT VRWSELDEQTQALYPQQNLRQPIRIVIDSQNRVTPVHRIV QQPGETWFARTQEDSREWPETVRTLLIPEHKGHLDLVVLX XQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPKL LGSDARGLCTLPGPQFKFKEIRHVGPDVCLHLVGA B:  TLYIQGQDEYYXARALKLAQRGRFTTHPNPNVGCVIVKDG EIVGEGYHQRAGEPHAEVHALRXAGEKAKGATAYVTLEPC SDALIAAGVARVVASXQDPNPQVAGRGLYRLQQAGIDVSH GLXXSEAEQLNKGFLKRXRTGFPYIQLKLGASLDGRTAXA SGESQWITSPQARRDVQLLRAQSHAILTSSATVLADDPAL TVRWSELDEQTQALYPQQNLRQPIRIVIDSQNRVTPVHRI VQQPGETWFARTQEDSREWPETVRTLLIPEHKGHLDLVVL XXQLGKQQINSIWVEAGPTLAGALLQAGLVDELIVYIAPK LLGSDARGLCTLPGLEKLADAPQFKFKEIRHVGPDVCLHL VGA Description (1)  Riboflavin biosynthesis protein ribD (E.C.1.1.1.193, 3.5.4.26) Functional site 1) chain A residue 50-88 type prosite sequence HAEVHALRXAGEKAKGATAYVTLEPCPCCDAL description CYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAEvhALrmagekakgatayvtle................PCshhgrtppCcdaL source prosite : PS00903 2) chain A residue 52 type ACT_SITE sequence E description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 52 type ACT_SITE sequence E description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 50 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 5) chain A residue 75 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 6) chain A residue 84 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 7) chain B residue 50 type BINDING sequence H description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 8) chain B residue 75 type BINDING sequence C description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 9) chain A residue 161 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 10) chain A residue 299 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 11) chain A residue 301 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 12) chain B residue 161 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 13) chain B residue 168 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 14) chain B residue 170 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 15) chain B residue 184 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 16) chain B residue 196 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 17) chain B residue 200 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 18) chain B residue 204 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 19) chain B residue 207 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 20) chain A residue 168 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 21) chain B residue 234 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 22) chain B residue 299 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 23) chain B residue 301 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 24) chain A residue 170 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 25) chain A residue 184 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 196 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 200 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 204 type BINDING sequence L description source Swiss-Prot : SWS_FT_FI3 29) chain A residue 207 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 30) chain A residue 234 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3

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