SitesBLAST
Comparing AO353_05970 FitnessBrowser__pseudo3_N2E3:AO353_05970 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)
72% identity, 94% coverage: 19:288/288 of query aligns to 30:299/299 of Q1LK00
- F68 (= F57) mutation to A: Abolishes catalytic activity.
- Y130 (= Y119) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R123) mutation to A: Abolishes catalytic activity.
- T271 (= T260) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
70% identity, 94% coverage: 19:288/288 of query aligns to 1:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F57), H43 (= H61), T46 (≠ S64), W90 (= W108), L93 (= L111), S112 (= S130), G113 (= G131), F114 (= F132), Y119 (= Y137), R120 (= R138), H228 (= H246), V232 (= V250), E242 (= E264), Y246 (= Y268), L247 (= L269)
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)
48% identity, 90% coverage: 30:288/288 of query aligns to 3:263/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F57), H36 (= H61), Y94 (= Y119), R98 (= R123), L101 (= L126), S104 (= S129), G234 (= G259), T235 (= T260)
- binding protoporphyrin ix containing fe: F32 (= F57), H36 (= H61), S39 (= S64), W83 (= W108), L86 (= L111), G106 (= G131), F107 (= F132), Y112 (= Y137), R113 (= R138), H221 (= H246), V225 (= V250), I229 (= I254), G234 (= G259), G236 (= G261), S238 (≠ T263)
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)
47% identity, 92% coverage: 25:288/288 of query aligns to 17:282/298 of Q8PDA8
- FIIQH 51:55 (= FIIQH 57:61) binding
- H55 (= H61) 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 (= Y119) binding
- R117 (= R123) binding
- H240 (= H246) binding axial binding residue
- T254 (= T260) binding
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
46% identity, 92% coverage: 25:288/288 of query aligns to 13:278/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H61), S54 (= S64), W98 (= W108), S120 (= S130), G121 (= G131), F122 (= F132), Y127 (= Y137), R128 (= R138), H236 (= H246), V240 (= V250), G249 (= G259), G251 (= G261), S253 (≠ T263)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F57), S51 (≠ H61), Y109 (= Y119), R113 (= R123), S119 (= S129), G249 (= G259), T250 (= T260)
- binding tryptophan: K82 (= K92), A85 (= A95), Y216 (= Y226), S217 (≠ Q227), E220 (= E230), D224 (= D234)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
43% identity, 90% coverage: 31:288/288 of query aligns to 1:241/243 of 1yw0A
5ti9C Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
32% identity, 84% coverage: 30:270/288 of query aligns to 1:287/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H61), Y40 (≠ S64), L93 (= L111), S112 (= S130), G113 (= G131), F114 (= F132), F119 (≠ Y137), R120 (= R138), W259 (= W242), H263 (= H246), V267 (= V250), M270 (≠ I253), G276 (= G259), G278 (= G261), S280 (≠ T263), L286 (= L269)
- binding N'-Formylkynurenine: F33 (= F57), H37 (= H61), R105 (= R123), L108 (= L126), A111 (≠ S129), S112 (= S130), G113 (= G131), L271 (≠ I254), G276 (= G259), T277 (= T260)
- binding tryptophan: R64 (≠ P88), E66 (≠ A90), W159 (vs. gap), R162 (vs. gap), T163 (vs. gap), P164 (vs. gap), I230 (≠ R213), F239 (≠ Y222), P242 (≠ L225)
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
29% identity, 84% coverage: 29:270/288 of query aligns to 1:294/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y32), Y7 (= Y35), F34 (= F57), H38 (= H61), A112 (≠ S129), S113 (= S130), T284 (= T260)
- binding protoporphyrin ix containing fe: H38 (= H61), Y41 (≠ S64), L94 (= L111), G114 (= G131), F115 (= F132), F120 (≠ Y137), R121 (= R138), H270 (= H246), M273 (≠ T249), V274 (= V250), M277 (≠ I253), G283 (= G259), G285 (= G261), S287 (≠ T263), Y292 (= Y268), L293 (= L269)
- binding alpha-methyl-L-tryptophan: R65 (≠ P88), E67 (≠ A90), W167 (≠ G186), R170 (vs. gap), T171 (vs. gap), P172 (vs. gap), F246 (≠ Y222)
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)
30% identity, 94% coverage: 4:273/288 of query aligns to 3:340/379 of P20351
- D123 (≠ E118) mutation to A: Strongly reduced enzyme activity.
- Y236 (vs. gap) mutation to F: Strongly reduced enzyme activity.
- R309 (= R243) mutation to A: Strongly reduced enzyme activity.
- H312 (= H246) binding axial binding residue
- Y335 (= Y268) mutation to F: Strongly reduced enzyme activity.
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
30% identity, 84% coverage: 32:273/288 of query aligns to 4:317/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H61), Y41 (≠ S64), F45 (≠ M68), L93 (= L111), F101 (≠ Y119), F114 (= F132), Q115 (= Q133), F119 (≠ Y137), Y136 (vs. gap), W285 (= W242), H289 (= H246), V293 (= V250), Y312 (= Y268), L313 (= L269)
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)
30% identity, 84% coverage: 29:270/288 of query aligns to 39:352/406 of P48775
- Y42 (= Y32) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y35) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F57) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIIQH 57:61) binding
- H76 (= H61) mutation to A: Abolishes enzyme activity.
- M108 (= M93) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y119) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R123) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S130) mutation to A: Reduces enzyme activity by 90%.
- Y175 (≠ L151) mutation to G: Reduces enzyme activity.
- H328 (= H246) binding axial binding residue; mutation to A: Abolishes enzyme activity.
- T342 (= T260) binding
5ti9A Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
30% identity, 84% coverage: 29:270/288 of query aligns to 1:314/350 of 5ti9A
- binding protoporphyrin ix containing fe: F34 (= F57), H38 (= H61), Y41 (≠ S64), F102 (≠ Y119), S113 (= S130), G114 (= G131), F115 (= F132), F120 (≠ Y137), R121 (= R138), W286 (= W242), H290 (= H246), M293 (≠ T249), V294 (= V250), G303 (= G259), G305 (= G261), S307 (≠ T263), L313 (= L269)
- binding tryptophan: F34 (= F57), H38 (= H61), R65 (≠ P88), E67 (≠ A90), F102 (≠ Y119), R106 (= R123), L109 (= L126), A112 (≠ S129), S113 (= S130), W170 (vs. gap), R173 (vs. gap), T174 (vs. gap), P175 (vs. gap), F266 (≠ Y222), P269 (≠ L225), G303 (= G259), T304 (= T260)
6pyzA Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
30% identity, 84% coverage: 29:270/288 of query aligns to 1:314/353 of 6pyzA
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y32), Y7 (= Y35), F34 (= F57), H38 (= H61), R106 (= R123), A112 (≠ S129), S113 (= S130), T304 (= T260)
- binding protoporphyrin ix containing fe: F34 (= F57), H38 (= H61), Y41 (≠ S64), L94 (= L111), F102 (≠ Y119), S113 (= S130), G114 (= G131), F115 (= F132), F120 (≠ Y137), R121 (= R138), H290 (= H246), M293 (≠ T249), V294 (= V250), M297 (≠ I253), G303 (= G259), G305 (= G261), S307 (≠ T263), Y312 (= Y268), L313 (= L269)
- binding alpha-methyl-L-tryptophan: R65 (≠ P88), E67 (≠ A90), W170 (vs. gap), R173 (vs. gap), T174 (vs. gap), P175 (vs. gap), F266 (≠ Y222), P269 (≠ L225)
6vbnA Crystal structure of htdo2 bound to inhibitor gne1 (see paper)
30% identity, 84% coverage: 30:270/288 of query aligns to 1:313/344 of 6vbnA
- binding protoporphyrin ix containing fe: H37 (= H61), Y40 (≠ S64), L93 (= L111), F101 (≠ Y119), S112 (= S130), G113 (= G131), F114 (= F132), F119 (≠ Y137), R120 (= R138), W285 (= W242), H289 (= H246), V293 (= V250), M296 (≠ I253), L297 (≠ I254), Y311 (= Y268), L312 (= L269)
- binding 1,5-anhydro-2,3-dideoxy-3-[(5S)-5H-imidazo[5,1-a]isoindol-5-yl]-D-threo-pentitol: Y3 (= Y32), Y6 (= Y35), F33 (= F57), H37 (= H61), L108 (= L126), A111 (≠ S129), G113 (= G131)
Q09474 Tryptophan 2,3-dioxygenase; TDO; Tryptamin 2,3-dioxygenase; Tryptophan oxygenase; TO; TRPO; Tryptophan pyrrolase; Tryptophanase; EC 1.13.11.11 from Caenorhabditis elegans (see paper)
27% identity, 87% coverage: 20:270/288 of query aligns to 29:351/403 of Q09474
- PLD 133:135 (≠ PTE 116:118) PLD motif; required for enzymatic activity; mutation Missing: Abolishes catalytic activity. Animals have an extended lifespan, an extended reproductive lifespan, have fewer hatched progeny and display increased motility.
6a4iD Crystal structure of human tdo inhibitor complex
32% identity, 78% coverage: 30:255/288 of query aligns to 1:248/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y32), Y6 (= Y35), F33 (= F57), H37 (= H61), A111 (≠ S129)
- binding protoporphyrin ix containing fe: F33 (= F57), H37 (= H61), Y40 (≠ S64), F101 (≠ Y119), S112 (= S130), G113 (= G131), F114 (= F132), F119 (≠ Y137), H239 (= H246), V243 (= V250), M246 (≠ I253)
- binding tryptophan: R64 (≠ P88), W153 (≠ I169), R156 (vs. gap), T157 (= T171), P158 (= P172), I206 (≠ R213), F215 (≠ Y222)
Sites not aligning to the query:
6a4iA Crystal structure of human tdo inhibitor complex
30% identity, 83% coverage: 32:270/288 of query aligns to 3:293/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y32), Y6 (= Y35), F33 (= F57), H37 (= H61), A111 (≠ S129)
- binding protoporphyrin ix containing fe: F33 (= F57), H37 (= H61), Y40 (≠ S64), L93 (= L111), F101 (≠ Y119), S112 (= S130), G113 (= G131), F114 (= F132), F119 (≠ Y137), W270 (= W242), H274 (= H246), M277 (≠ T249), V278 (= V250), M281 (≠ I253), L292 (= L269)
- binding tryptophan: R64 (≠ P88), W158 (vs. gap), R161 (vs. gap), T162 (vs. gap), P163 (vs. gap), I241 (≠ R213), F250 (≠ Y222), P253 (≠ L225)
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
31% identity, 78% coverage: 30:255/288 of query aligns to 1:272/310 of 8qv7B
Sites not aligning to the query:
6a4iB Crystal structure of human tdo inhibitor complex
30% identity, 78% coverage: 30:255/288 of query aligns to 1:268/309 of 6a4iB
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y32), Y6 (= Y35), F33 (= F57), H37 (= H61), L108 (= L126), A111 (≠ S129)
- binding protoporphyrin ix containing fe: F33 (= F57), H37 (= H61), Y40 (≠ S64), L93 (= L111), S112 (= S130), G113 (= G131), F114 (= F132), F119 (≠ Y137), R120 (= R138), W255 (= W242), H259 (= H246), V263 (= V250)
- binding tryptophan: R64 (≠ P88), E66 (≠ A90), W153 (≠ A168), R156 (vs. gap), T157 (= T171), P158 (= P172), P238 (≠ L225)
Sites not aligning to the query:
8r5qC Structure of apo tdo with a bound inhibitor
29% identity, 78% coverage: 30:255/288 of query aligns to 1:282/317 of 8r5qC
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y32), Y6 (= Y35), L7 (= L36), F33 (= F57), H37 (= H61), F101 (≠ Y119), P110 (≠ Q128), G113 (= G131), Q115 (= Q133), S116 (= S134), H273 (= H246), V277 (= V250), M280 (≠ I253)
- binding alpha-methyl-L-tryptophan: R64 (≠ P88), E66 (≠ A90), W153 (vs. gap), R156 (vs. gap), P158 (vs. gap), F249 (≠ Y222)
Query Sequence
>AO353_05970 FitnessBrowser__pseudo3_N2E3:AO353_05970
MSQCPYSSDQSPSNPPEEWHNAELNFSDSMSYGDYLDLGKILSAQHPLSPDHNEMLFIIQ
HQTSELWMKLMLHELKAAREHVRLGELPPAFKMLARVSRIFDQLVHAWTVLATMTPTEYH
AIRPFLGQSSGFQSFQYREIEFILGNKSATLLRPHAHRPELLAELEKAIATPSLYDESIR
LMVSAGLAIDPQRFERDPASPTAYDASVEAAWRVVYTDPSRYWDLYQLAEKLIDLEDSFR
QWRFRHVTTVERIIGFQPGTGGTEGVGYLRKMLDTVLFPELWRVRSTL
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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