SitesBLAST
Comparing BPHYT_RS16035 FitnessBrowser__BFirm:BPHYT_RS16035 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
Q1LK00 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans) (see paper)
71% identity, 95% coverage: 17:310/310 of query aligns to 5:299/299 of Q1LK00
- F68 (= F79) mutation to A: Abolishes catalytic activity.
- Y130 (= Y141) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R145) mutation to A: Abolishes catalytic activity.
- T271 (= T282) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
73% identity, 87% coverage: 41:310/310 of query aligns to 1:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F79), H43 (= H83), T46 (≠ S86), W90 (= W130), L93 (= L133), S112 (= S152), G113 (= G153), F114 (= F154), Y119 (= Y159), R120 (= R160), H228 (= H268), V232 (= V272), E242 (≠ S286), Y246 (= Y290), L247 (= L291)
Q8PDA8 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) (see 2 papers)
52% identity, 85% coverage: 47:308/310 of query aligns to 17:280/298 of Q8PDA8
- FIIQH 51:55 (= FIIQH 79:83) binding
- H55 (= H83) mutation to A: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate.; mutation to S: Decrease in catalytic efficiency using L-tryptophan, 5-fluoro-D/L-tryptophan, 6-fluoro-D/L-tryptophan, 5-methyl-D/L-tryptophan and 6-methyl-D/L-tryptophan as substrate.
- Y113 (= Y141) binding
- R117 (= R145) binding
- H240 (= H268) binding axial binding residue
- T254 (= T282) binding
2nw9A Crystal structure of tryptophan 2,3-dioxygenase (tdo) from xanthomonas campestris in complex with ferrous heme and 6-fluoro-tryptophan. Northeast structural genomics target xcr13 (see paper)
52% identity, 83% coverage: 52:308/310 of query aligns to 3:261/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F79), H36 (= H83), Y94 (= Y141), R98 (= R145), L101 (= L148), S104 (= S151), G234 (= G281), T235 (= T282)
- binding protoporphyrin ix containing fe: F32 (= F79), H36 (= H83), S39 (= S86), W83 (= W130), L86 (= L133), G106 (= G153), F107 (= F154), Y112 (= Y159), R113 (= R160), H221 (= H268), V225 (= V272), I229 (= I276), G234 (= G281), G236 (= G283), S238 (≠ T285)
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
51% identity, 85% coverage: 47:308/310 of query aligns to 13:276/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H83), S54 (= S86), W98 (= W130), S120 (= S152), G121 (= G153), F122 (= F154), Y127 (= Y159), R128 (= R160), H236 (= H268), V240 (= V272), G249 (= G281), G251 (= G283), S253 (≠ T285)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F79), S51 (≠ H83), Y109 (= Y141), R113 (= R145), S119 (= S151), G249 (= G281), T250 (= T282)
- binding tryptophan: K82 (= K114), A85 (= A117), Y216 (= Y248), S217 (≠ E249), E220 (= E252), D224 (= D256)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
48% identity, 83% coverage: 53:308/310 of query aligns to 1:239/243 of 1yw0A
P20351 Tryptophan 2,3-dioxygenase; TDO; Protein vermilion; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Drosophila melanogaster (Fruit fly) (see paper)
31% identity, 91% coverage: 30:310/310 of query aligns to 1:357/379 of P20351
- D123 (≠ E140) mutation to A: Strongly reduced enzyme activity.
- Y236 (vs. gap) mutation to F: Strongly reduced enzyme activity.
- R309 (= R265) mutation to A: Strongly reduced enzyme activity.
- H312 (= H268) binding axial binding residue
- Y335 (= Y290) mutation to F: Strongly reduced enzyme activity.
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
32% identity, 83% coverage: 54:310/310 of query aligns to 4:334/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H83), Y41 (≠ S86), F45 (≠ M90), L93 (= L133), F101 (≠ Y141), F114 (= F154), Q115 (= Q155), F119 (≠ Y159), Y136 (≠ P176), W285 (= W264), H289 (= H268), V293 (= V272), Y312 (= Y290), L313 (= L291)
5ti9C Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
31% identity, 84% coverage: 52:310/310 of query aligns to 1:307/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H83), Y40 (≠ S86), L93 (= L133), S112 (= S152), G113 (= G153), F114 (= F154), F119 (≠ Y159), R120 (= R160), W259 (= W264), H263 (= H268), V267 (= V272), M270 (≠ I275), G276 (= G281), G278 (= G283), S280 (≠ T285), L286 (= L291)
- binding N'-Formylkynurenine: F33 (= F79), H37 (= H83), R105 (= R145), L108 (= L148), A111 (≠ S151), S112 (= S152), G113 (= G153), L271 (≠ I276), G276 (= G281), T277 (= T282)
- binding tryptophan: R64 (= R106), E66 (= E108), W159 (≠ S190), R162 (≠ A193), T163 (≠ P194), P164 (vs. gap), I230 (≠ L235), F239 (≠ H244), P242 (≠ L247)
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
30% identity, 84% coverage: 52:310/310 of query aligns to 2:314/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y54), Y7 (= Y57), F34 (= F79), H38 (= H83), A112 (≠ S151), S113 (= S152), T284 (= T282)
- binding protoporphyrin ix containing fe: H38 (= H83), Y41 (≠ S86), L94 (= L133), G114 (= G153), F115 (= F154), F120 (≠ Y159), R121 (= R160), H270 (= H268), M273 (≠ T271), V274 (= V272), M277 (≠ I275), G283 (= G281), G285 (= G283), S287 (≠ T285), Y292 (= Y290), L293 (= L291)
- binding alpha-methyl-L-tryptophan: R65 (= R106), E67 (= E108), W167 (≠ Y197), R170 (≠ V200), T171 (≠ V201), P172 (≠ R202), F246 (≠ H244)
6a4iD Crystal structure of human tdo inhibitor complex
33% identity, 74% coverage: 52:279/310 of query aligns to 1:250/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y54), Y6 (= Y57), F33 (= F79), H37 (= H83), A111 (≠ S151)
- binding protoporphyrin ix containing fe: F33 (= F79), H37 (= H83), Y40 (≠ S86), F101 (≠ Y141), S112 (= S152), G113 (= G153), F114 (= F154), F119 (≠ Y159), H239 (= H268), V243 (= V272), M246 (≠ I275)
- binding tryptophan: R64 (= R106), W153 (≠ S190), R156 (≠ A193), T157 (≠ P194), P158 (vs. gap), I206 (≠ L235), F215 (≠ H244)
Sites not aligning to the query:
6a4iB Crystal structure of human tdo inhibitor complex
30% identity, 84% coverage: 52:310/310 of query aligns to 1:295/309 of 6a4iB
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y54), Y6 (= Y57), F33 (= F79), H37 (= H83), L108 (= L148), A111 (≠ S151)
- binding protoporphyrin ix containing fe: F33 (= F79), H37 (= H83), Y40 (≠ S86), L93 (= L133), S112 (= S152), G113 (= G153), F114 (= F154), F119 (≠ Y159), R120 (= R160), W255 (= W264), H259 (= H268), V263 (= V272), L274 (= L291)
- binding tryptophan: R64 (= R106), E66 (= E108), W153 (≠ S190), R156 (≠ A193), T157 (≠ P194), P158 (vs. gap), P238 (≠ L247)
6a4iA Crystal structure of human tdo inhibitor complex
29% identity, 84% coverage: 52:310/310 of query aligns to 1:313/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y54), Y6 (= Y57), F33 (= F79), H37 (= H83), A111 (≠ S151)
- binding protoporphyrin ix containing fe: F33 (= F79), H37 (= H83), Y40 (≠ S86), L93 (= L133), F101 (≠ Y141), S112 (= S152), G113 (= G153), F114 (= F154), F119 (≠ Y159), W270 (= W264), H274 (= H268), M277 (≠ T271), V278 (= V272), M281 (≠ I275), L292 (= L291)
- binding tryptophan: R64 (= R106), W158 (≠ S190), R161 (≠ A193), T162 (≠ P194), P163 (vs. gap), I241 (≠ L235), F250 (≠ H244), P253 (≠ L247)
8r5qC Structure of apo tdo with a bound inhibitor
29% identity, 77% coverage: 52:291/310 of query aligns to 1:298/317 of 8r5qC
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y54), Y6 (= Y57), L7 (= L58), F33 (= F79), H37 (= H83), F101 (≠ Y141), P110 (≠ S150), G113 (= G153), Q115 (= Q155), S116 (= S156), H273 (= H268), V277 (= V272), M280 (≠ I275)
- binding alpha-methyl-L-tryptophan: R64 (= R106), E66 (= E108), W153 (≠ S190), R156 (≠ A193), P158 (vs. gap), F249 (≠ H244)
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
30% identity, 73% coverage: 52:277/310 of query aligns to 1:272/310 of 8qv7B
Sites not aligning to the query:
8r5qA Structure of apo tdo with a bound inhibitor
29% identity, 77% coverage: 52:291/310 of query aligns to 1:298/314 of 8r5qA
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y54), Y6 (= Y57), L7 (= L58), F33 (= F79), H37 (= H83), F101 (≠ Y141), P110 (≠ S150), G113 (= G153), F114 (= F154), Q115 (= Q155), S116 (= S156), H274 (= H268), V278 (= V272), M281 (≠ I275)
- binding alpha-methyl-L-tryptophan: R64 (= R106), E66 (= E108), W154 (≠ S190), R157 (≠ A193), T158 (≠ P194), P159 (vs. gap), F250 (≠ H244)
7lu7CCC Tryptophan 2,3-dioxygenase
29% identity, 73% coverage: 52:277/310 of query aligns to 2:279/323 of 7lu7CCC
- binding (1~{R})-1-cyclohexyl-2-[(5~{S})-5~{H}-imidazo[1,5-b]isoindol-5-yl]ethanol: Y4 (= Y54), Y7 (= Y57), F34 (= F79), H38 (= H83), A112 (≠ S151), G114 (= G153)
- binding protoporphyrin ix containing fe: H38 (= H83), Y41 (≠ S86), S113 (= S152), G114 (= G153), F115 (= F154), F120 (≠ Y159), R121 (= R160), W266 (= W264), H270 (= H268), V274 (= V272)
- binding alpha-methyl-L-tryptophan: R65 (= R106), E67 (= E108), W163 (≠ S190), R166 (≠ A193), T167 (≠ P194), P168 (vs. gap), F246 (≠ H244), P249 (≠ L247)
8r5qB Structure of apo tdo with a bound inhibitor
29% identity, 77% coverage: 52:291/310 of query aligns to 1:299/318 of 8r5qB
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y54), Y6 (= Y57), L7 (= L58), F33 (= F79), H37 (= H83), F101 (≠ Y141), P110 (≠ S150), G113 (= G153), Q115 (= Q155), S116 (= S156), H275 (= H268), V279 (= V272), M282 (≠ I275)
- binding alpha-methyl-L-tryptophan: R64 (= R106), E66 (= E108), W155 (≠ S190), R158 (≠ A193), P160 (vs. gap), F251 (≠ H244)
P48775 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Homo sapiens (Human) (see 3 papers)
37% identity, 48% coverage: 18:167/310 of query aligns to 3:166/406 of P48775
- Y42 (= Y54) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y57) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F79) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIIQH 79:83) binding
- H76 (= H83) mutation to A: Abolishes enzyme activity.
- M108 (≠ L109) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y141) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R145) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S152) mutation to A: Reduces enzyme activity by 90%.
Sites not aligning to the query:
- 175 Y→G: Reduces enzyme activity.
- 328 binding axial binding residue; H→A: Abolishes enzyme activity.
- 342 binding
7lu7AAA Tryptophan 2,3-dioxygenase
40% identity, 44% coverage: 52:186/310 of query aligns to 2:146/341 of 7lu7AAA
- binding (1~{R})-1-cyclohexyl-2-[(5~{S})-5~{H}-imidazo[1,5-b]isoindol-5-yl]ethanol: Y4 (= Y54), Y7 (= Y57), F34 (= F79), H38 (= H83), A112 (≠ S151), G114 (= G153)
- binding protoporphyrin ix containing fe: F34 (= F79), H38 (= H83), Y41 (≠ S86), L94 (= L133), S113 (= S152), G114 (= G153), F115 (= F154), F120 (≠ Y159), R121 (= R160)
- binding alpha-methyl-L-tryptophan: R65 (= R106), E67 (= E108)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS16035 FitnessBrowser__BFirm:BPHYT_RS16035
MTDHMQTPGLPEEKPAQGCPFGHGAVASSVATPAADSGDGWHDAQLDFSESMSYGDYLSL
GTVLDAQHPLSPDHNEMLFIIQHQTSELWMKLALYELRAALQAVHRDELPPAFKMLARVS
RIMEQLVQAWSVLATMTPSEYTAMRPYLGSSSGFQSYQYRQIEFLLGNKNEQMLKPHAHR
ADVLAEVKASLEAPSFYDEVVRLLARRGFAISAARLERDWTQPTVHDASVEAAWLEVYRN
PSQHWELYEMAEELVDLEDAFRQWRFRHVTTVERIIGFKQGTGGTSGATYLRKMLDVVLF
PELWHVRTML
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory