SitesBLAST
Comparing RR42_RS15390 FitnessBrowser__Cup4G11:RR42_RS15390 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)
82% identity, 100% coverage: 1:291/291 of query aligns to 1:299/299 of Q1LK00
- F68 (= F60) mutation to A: Abolishes catalytic activity.
- Y130 (= Y122) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R126) mutation to A: Abolishes catalytic activity.
- T271 (= T263) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
86% identity, 93% coverage: 22:291/291 of query aligns to 1:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F60), H43 (= H64), T46 (≠ S67), W90 (= W111), L93 (= L114), S112 (= S133), G113 (= G134), F114 (= F135), Y119 (= Y140), R120 (= R141), H228 (= H249), V232 (= V253), E242 (= E267), Y246 (= Y271), L247 (= L272)
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)
49% identity, 91% coverage: 28:291/291 of query aligns to 17:282/298 of Q8PDA8
- FIIQH 51:55 (≠ FIVQH 60:64) binding
- H55 (= H64) 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 (= Y122) binding
- R117 (= R126) binding
- H240 (= H249) binding axial binding residue
- T254 (= T263) 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)
49% identity, 89% coverage: 33:291/291 of query aligns to 3:263/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F60), H36 (= H64), Y94 (= Y122), R98 (= R126), L101 (= L129), S104 (= S132), G234 (= G262), T235 (= T263)
- binding protoporphyrin ix containing fe: F32 (= F60), H36 (= H64), S39 (= S67), W83 (= W111), L86 (= L114), G106 (= G134), F107 (= F135), Y112 (= Y140), R113 (= R141), H221 (= H249), V225 (= V253), I229 (= I257), G234 (= G262), G236 (= G264), S238 (≠ T266)
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
48% identity, 91% coverage: 28:291/291 of query aligns to 13:278/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H64), S54 (= S67), W98 (= W111), S120 (= S133), G121 (= G134), F122 (= F135), Y127 (= Y140), R128 (= R141), H236 (= H249), V240 (= V253), G249 (= G262), G251 (= G264), S253 (≠ T266)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F60), S51 (≠ H64), Y109 (= Y122), R113 (= R126), S119 (= S132), G249 (= G262), T250 (= T263)
- binding tryptophan: K82 (= K95), A85 (≠ T98), Y216 (= Y229), S217 (≠ E230), E220 (= E233), D224 (= D237)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
45% identity, 89% coverage: 34:291/291 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)
30% identity, 89% coverage: 33:291/291 of query aligns to 1:307/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H64), Y40 (≠ S67), L93 (= L114), S112 (= S133), G113 (= G134), F114 (= F135), F119 (≠ Y140), R120 (= R141), W259 (= W245), H263 (= H249), V267 (= V253), M270 (≠ V256), G276 (= G262), G278 (= G264), S280 (≠ T266), L286 (= L272)
- binding N'-Formylkynurenine: F33 (= F60), H37 (= H64), R105 (= R126), L108 (= L129), A111 (≠ S132), S112 (= S133), G113 (= G134), L271 (≠ I257), G276 (= G262), T277 (= T263)
- binding tryptophan: R64 (≠ P91), E66 (≠ A93), W159 (≠ L172), R162 (= R173), T163 (= T174), P164 (= P175), I230 (≠ E217), F239 (≠ W226), P242 (vs. gap)
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)
29% identity, 98% coverage: 6:289/291 of query aligns to 2:355/379 of P20351
- D123 (≠ E121) mutation to A: Strongly reduced enzyme activity.
- Y236 (≠ V211) mutation to F: Strongly reduced enzyme activity.
- R309 (= R246) mutation to A: Strongly reduced enzyme activity.
- H312 (= H249) binding axial binding residue
- Y335 (= Y271) mutation to F: Strongly reduced enzyme activity.
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
30% identity, 89% coverage: 33:291/291 of query aligns to 2:314/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y35), Y7 (= Y38), F34 (= F60), H38 (= H64), A112 (≠ S132), S113 (= S133), T284 (= T263)
- binding protoporphyrin ix containing fe: H38 (= H64), Y41 (≠ S67), L94 (= L114), G114 (= G134), F115 (= F135), F120 (≠ Y140), R121 (= R141), H270 (= H249), M273 (≠ T252), V274 (= V253), M277 (≠ V256), G283 (= G262), G285 (= G264), S287 (≠ T266), Y292 (= Y271), L293 (= L272)
- binding alpha-methyl-L-tryptophan: R65 (≠ P91), E67 (≠ A93), W167 (≠ L172), R170 (= R173), T171 (= T174), P172 (= P175), F246 (≠ W226)
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
29% identity, 88% coverage: 35:291/291 of query aligns to 4:334/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H64), Y41 (≠ S67), F45 (≠ M71), L93 (= L114), F101 (≠ Y122), F114 (= F135), Q115 (= Q136), F119 (≠ Y140), Y136 (vs. gap), W285 (= W245), H289 (= H249), V293 (= V253), Y312 (= Y271), L313 (= L272)
6a4iD Crystal structure of human tdo inhibitor complex
31% identity, 78% coverage: 33:260/291 of query aligns to 1:250/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y35), Y6 (= Y38), F33 (= F60), H37 (= H64), A111 (≠ S132)
- binding protoporphyrin ix containing fe: F33 (= F60), H37 (= H64), Y40 (≠ S67), F101 (≠ Y122), S112 (= S133), G113 (= G134), F114 (= F135), F119 (≠ Y140), H239 (= H249), V243 (= V253), M246 (≠ V256)
- binding tryptophan: R64 (≠ P91), W153 (≠ L172), R156 (= R173), T157 (= T174), P158 (= P175), I206 (≠ E217), F215 (≠ W226)
Sites not aligning to the query:
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)
25% identity, 98% coverage: 6:289/291 of query aligns to 2:369/403 of Q09474
- PLD 133:135 (≠ PPE 119:121) 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.
6a4iB Crystal structure of human tdo inhibitor complex
29% identity, 89% coverage: 33:291/291 of query aligns to 1:295/309 of 6a4iB
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y35), Y6 (= Y38), F33 (= F60), H37 (= H64), L108 (= L129), A111 (≠ S132)
- binding protoporphyrin ix containing fe: F33 (= F60), H37 (= H64), Y40 (≠ S67), L93 (= L114), S112 (= S133), G113 (= G134), F114 (= F135), F119 (≠ Y140), R120 (= R141), W255 (= W245), H259 (= H249), V263 (= V253), L274 (= L272)
- binding tryptophan: R64 (≠ P91), E66 (≠ A93), W153 (≠ L172), R156 (= R173), T157 (= T174), P158 (= P175), P238 (vs. gap)
6a4iA Crystal structure of human tdo inhibitor complex
27% identity, 89% coverage: 33:291/291 of query aligns to 1:313/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y35), Y6 (= Y38), F33 (= F60), H37 (= H64), A111 (≠ S132)
- binding protoporphyrin ix containing fe: F33 (= F60), H37 (= H64), Y40 (≠ S67), L93 (= L114), F101 (≠ Y122), S112 (= S133), G113 (= G134), F114 (= F135), F119 (≠ Y140), W270 (= W245), H274 (= H249), M277 (≠ T252), V278 (= V253), M281 (≠ V256), L292 (= L272)
- binding tryptophan: R64 (≠ P91), W158 (≠ A171), R161 (= R173), T162 (= T174), P163 (= P175), I241 (≠ E217), F250 (≠ W226), P253 (vs. gap)
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
28% identity, 78% coverage: 33:258/291 of query aligns to 1:272/310 of 8qv7B
Sites not aligning to the query:
8r5qC Structure of apo tdo with a bound inhibitor
38% identity, 50% coverage: 33:177/291 of query aligns to 1:160/317 of 8r5qC
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y35), Y6 (= Y38), L7 (= L39), F33 (= F60), H37 (= H64), F101 (≠ Y122), P110 (≠ M131), G113 (= G134), Q115 (= Q136), S116 (= S137)
- binding alpha-methyl-L-tryptophan: R64 (≠ P91), E66 (≠ A93), W153 (≠ L172), R156 (= R173), P158 (= P175)
Sites not aligning to the query:
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)
35% identity, 49% coverage: 6:148/291 of query aligns to 3:166/406 of P48775
- Y42 (= Y35) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y38) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F60) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIVQH 60:64) binding
- H76 (= H64) mutation to A: Abolishes enzyme activity.
- M108 (= M96) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y122) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R126) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S133) 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
7lu7CCC Tryptophan 2,3-dioxygenase
28% identity, 78% coverage: 33:258/291 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 (= Y35), Y7 (= Y38), F34 (= F60), H38 (= H64), A112 (≠ S132), G114 (= G134)
- binding protoporphyrin ix containing fe: H38 (= H64), Y41 (≠ S67), S113 (= S133), G114 (= G134), F115 (= F135), F120 (≠ Y140), R121 (= R141), W266 (= W245), H270 (= H249), V274 (= V253)
- binding alpha-methyl-L-tryptophan: R65 (≠ P91), E67 (≠ A93), W163 (≠ L172), R166 (= R173), T167 (= T174), P168 (= P175), F246 (≠ W226), P249 (vs. gap)
8r5qA Structure of apo tdo with a bound inhibitor
38% identity, 50% coverage: 33:177/291 of query aligns to 1:161/314 of 8r5qA
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y35), Y6 (= Y38), L7 (= L39), F33 (= F60), H37 (= H64), F101 (≠ Y122), P110 (≠ M131), G113 (= G134), F114 (= F135), Q115 (= Q136), S116 (= S137)
- binding alpha-methyl-L-tryptophan: R64 (≠ P91), E66 (≠ A93), W154 (≠ L172), R157 (= R173), T158 (= T174), P159 (= P175)
Sites not aligning to the query:
8r5qB Structure of apo tdo with a bound inhibitor
38% identity, 50% coverage: 33:177/291 of query aligns to 1:162/318 of 8r5qB
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y35), Y6 (= Y38), L7 (= L39), F33 (= F60), H37 (= H64), F101 (≠ Y122), P110 (≠ M131), G113 (= G134), Q115 (= Q136), S116 (= S137)
- binding alpha-methyl-L-tryptophan: R64 (≠ P91), E66 (≠ A93), W155 (≠ L172), R158 (= R173), P160 (= P175)
Sites not aligning to the query:
Query Sequence
>RR42_RS15390 FitnessBrowser__Cup4G11:RR42_RS15390
MSNHKGCPMSGAGATETSDASWHDAQMDFAKDMSYGDYLALDQILNAQHPLSPEHNEMLF
IVQHQTSELWMKLALHELRAARECVRQDQLPPAFKMLTRVSRIMEQLVQAWNVLATMTPP
EYSAMRPYLGMSSGFQSFQYREIEFILGNKNAAMLRPHAHQPQHLALLEEALRTPSLYDE
AIRLMARRGFAIDAACIERDWTRPAGENASVEAAWLEVYRKPEAHWELYELGEKFVDLED
AFRQWRFRHVTTVERVIGFKRGTGGTEGVSYLRKMLDVVLFPELWKLRTDL
Or try a new SitesBLAST search
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