SitesBLAST
Comparing H281DRAFT_04144 FitnessBrowser__Burk376:H281DRAFT_04144 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: 17:313/313 of query aligns to 5:299/299 of Q1LK00
- F68 (= F82) mutation to A: Abolishes catalytic activity.
- Y130 (= Y144) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R148) mutation to A: Abolishes catalytic activity.
- T271 (= T285) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
73% identity, 86% coverage: 44:313/313 of query aligns to 1:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F82), H43 (= H86), T46 (≠ S89), W90 (= W133), L93 (= L136), S112 (= S155), G113 (= G156), F114 (= F157), Y119 (= Y162), R120 (= R163), H228 (= H271), V232 (= V275), E242 (≠ S289), Y246 (= Y293), L247 (= L294)
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)
51% identity, 84% coverage: 50:311/313 of query aligns to 17:280/298 of Q8PDA8
- FIIQH 51:55 (= FIIQH 82:86) binding
- H55 (= H86) 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 (= Y144) binding
- R117 (= R148) binding
- H240 (= H271) binding axial binding residue
- T254 (= T285) 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)
51% identity, 82% coverage: 55:311/313 of query aligns to 3:261/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F82), H36 (= H86), Y94 (= Y144), R98 (= R148), L101 (= L151), S104 (= S154), G234 (= G284), T235 (= T285)
- binding protoporphyrin ix containing fe: F32 (= F82), H36 (= H86), S39 (= S89), W83 (= W133), L86 (= L136), G106 (= G156), F107 (= F157), Y112 (= Y162), R113 (= R163), H221 (= H271), V225 (= V275), I229 (= I279), G234 (= G284), G236 (= G286), S238 (≠ T288)
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
50% identity, 84% coverage: 50:311/313 of query aligns to 13:276/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H86), S54 (= S89), W98 (= W133), S120 (= S155), G121 (= G156), F122 (= F157), Y127 (= Y162), R128 (= R163), H236 (= H271), V240 (= V275), G249 (= G284), G251 (= G286), S253 (≠ T288)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F82), S51 (≠ H86), Y109 (= Y144), R113 (= R148), S119 (= S154), G249 (= G284), T250 (= T285)
- binding tryptophan: K82 (= K117), A85 (= A120), Y216 (= Y251), S217 (≠ E252), E220 (= E255), D224 (= D259)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
47% identity, 82% coverage: 56:311/313 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)
30% identity, 95% coverage: 18:313/313 of query aligns to 2:357/379 of P20351
- D123 (≠ E143) mutation to A: Strongly reduced enzyme activity.
- Y236 (vs. gap) mutation to F: Strongly reduced enzyme activity.
- R309 (= R268) mutation to A: Strongly reduced enzyme activity.
- H312 (= H271) binding axial binding residue
- Y335 (= Y293) mutation to F: Strongly reduced enzyme activity.
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
31% identity, 82% coverage: 57:313/313 of query aligns to 4:334/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H86), Y41 (≠ S89), F45 (≠ M93), L93 (= L136), F101 (≠ Y144), F114 (= F157), Q115 (= Q158), F119 (≠ Y162), Y136 (≠ P179), W285 (= W267), H289 (= H271), V293 (= V275), Y312 (= Y293), L313 (= L294)
5ti9C Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
30% identity, 83% coverage: 55:313/313 of query aligns to 1:307/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H86), Y40 (≠ S89), L93 (= L136), S112 (= S155), G113 (= G156), F114 (= F157), F119 (≠ Y162), R120 (= R163), W259 (= W267), H263 (= H271), V267 (= V275), M270 (≠ I278), G276 (= G284), G278 (= G286), S280 (≠ T288), L286 (= L294)
- binding N'-Formylkynurenine: F33 (= F82), H37 (= H86), R105 (= R148), L108 (= L151), A111 (≠ S154), S112 (= S155), G113 (= G156), L271 (≠ I279), G276 (= G284), T277 (= T285)
- binding tryptophan: R64 (= R109), E66 (= E111), W159 (≠ S193), R162 (vs. gap), T163 (vs. gap), P164 (vs. gap), I230 (≠ L238), F239 (≠ H247), P242 (≠ L250)
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
30% identity, 83% coverage: 55:313/313 of query aligns to 2:314/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y57), Y7 (= Y60), F34 (= F82), H38 (= H86), A112 (≠ S154), S113 (= S155), T284 (= T285)
- binding protoporphyrin ix containing fe: H38 (= H86), Y41 (≠ S89), L94 (= L136), G114 (= G156), F115 (= F157), F120 (≠ Y162), R121 (= R163), H270 (= H271), M273 (≠ T274), V274 (= V275), M277 (≠ I278), G283 (= G284), G285 (= G286), S287 (≠ T288), Y292 (= Y293), L293 (= L294)
- binding alpha-methyl-L-tryptophan: R65 (= R109), E67 (= E111), W167 (≠ L207), R170 (= R210), T171 (≠ G211), P172 (≠ F212), F246 (≠ H247)
6a4iD Crystal structure of human tdo inhibitor complex
32% identity, 73% coverage: 55:282/313 of query aligns to 1:250/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y57), Y6 (= Y60), F33 (= F82), H37 (= H86), A111 (≠ S154)
- binding protoporphyrin ix containing fe: F33 (= F82), H37 (= H86), Y40 (≠ S89), F101 (≠ Y144), S112 (= S155), G113 (= G156), F114 (= F157), F119 (≠ Y162), H239 (= H271), V243 (= V275), M246 (≠ I278)
- binding tryptophan: R64 (= R109), W153 (≠ S193), R156 (≠ S196), T157 (≠ P197), P158 (vs. gap), I206 (≠ L238), F215 (≠ H247)
Sites not aligning to the query:
6a4iB Crystal structure of human tdo inhibitor complex
30% identity, 83% coverage: 55:313/313 of query aligns to 1:295/309 of 6a4iB
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y57), Y6 (= Y60), F33 (= F82), H37 (= H86), L108 (= L151), A111 (≠ S154)
- binding protoporphyrin ix containing fe: F33 (= F82), H37 (= H86), Y40 (≠ S89), L93 (= L136), S112 (= S155), G113 (= G156), F114 (= F157), F119 (≠ Y162), R120 (= R163), W255 (= W267), H259 (= H271), V263 (= V275), L274 (= L294)
- binding tryptophan: R64 (= R109), E66 (= E111), W153 (≠ S193), R156 (≠ S196), T157 (≠ P197), P158 (vs. gap), P238 (≠ L250)
6a4iA Crystal structure of human tdo inhibitor complex
28% identity, 83% coverage: 55:313/313 of query aligns to 1:313/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y57), Y6 (= Y60), F33 (= F82), H37 (= H86), A111 (≠ S154)
- binding protoporphyrin ix containing fe: F33 (= F82), H37 (= H86), Y40 (≠ S89), L93 (= L136), F101 (≠ Y144), S112 (= S155), G113 (= G156), F114 (= F157), F119 (≠ Y162), W270 (= W267), H274 (= H271), M277 (≠ T274), V278 (= V275), M281 (≠ I278), L292 (= L294)
- binding tryptophan: R64 (= R109), W158 (≠ S193), R161 (≠ S196), T162 (≠ P197), P163 (vs. gap), I241 (vs. gap), F250 (vs. gap), P253 (vs. gap)
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
29% identity, 72% coverage: 55:280/313 of query aligns to 1:272/310 of 8qv7B
Sites not aligning to the query:
7lu7CCC Tryptophan 2,3-dioxygenase
29% identity, 72% coverage: 55:280/313 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 (= Y57), Y7 (= Y60), F34 (= F82), H38 (= H86), A112 (≠ S154), G114 (= G156)
- binding protoporphyrin ix containing fe: H38 (= H86), Y41 (≠ S89), S113 (= S155), G114 (= G156), F115 (= F157), F120 (≠ Y162), R121 (= R163), W266 (= W267), H270 (= H271), V274 (= V275)
- binding alpha-methyl-L-tryptophan: R65 (= R109), E67 (= E111), W163 (≠ S193), R166 (≠ S196), T167 (≠ P197), P168 (vs. gap), F246 (≠ H247), P249 (≠ L250)
8r5qC Structure of apo tdo with a bound inhibitor
29% identity, 72% coverage: 55:280/313 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 (= Y57), Y6 (= Y60), L7 (= L61), F33 (= F82), H37 (= H86), F101 (≠ Y144), P110 (≠ S153), G113 (= G156), Q115 (= Q158), S116 (= S159), H273 (= H271), V277 (= V275), M280 (≠ I278)
- binding alpha-methyl-L-tryptophan: R64 (= R109), E66 (= E111), W153 (≠ S193), R156 (vs. gap), P158 (vs. gap), F249 (≠ H247)
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)
38% identity, 49% coverage: 18:170/313 of query aligns to 3:166/406 of P48775
- Y42 (= Y57) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y60) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F82) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIIQH 82:86) binding
- H76 (= H86) mutation to A: Abolishes enzyme activity.
- M108 (≠ L112) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y144) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R148) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S155) 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
8r5qA Structure of apo tdo with a bound inhibitor
28% identity, 72% coverage: 55:280/313 of query aligns to 1:283/314 of 8r5qA
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y57), Y6 (= Y60), L7 (= L61), F33 (= F82), H37 (= H86), F101 (≠ Y144), P110 (≠ S153), G113 (= G156), F114 (= F157), Q115 (= Q158), S116 (= S159), H274 (= H271), V278 (= V275), M281 (≠ I278)
- binding alpha-methyl-L-tryptophan: R64 (= R109), E66 (= E111), W154 (≠ S193), R157 (vs. gap), T158 (vs. gap), P159 (vs. gap), F250 (≠ H247)
8r5qB Structure of apo tdo with a bound inhibitor
28% identity, 72% coverage: 55:280/313 of query aligns to 1:284/318 of 8r5qB
- binding 3-chloranyl-~{N}-[(1~{S})-1-(6-chloranylpyridin-3-yl)-2-phenyl-ethyl]aniline: Y3 (= Y57), Y6 (= Y60), L7 (= L61), F33 (= F82), H37 (= H86), F101 (≠ Y144), P110 (≠ S153), G113 (= G156), Q115 (= Q158), S116 (= S159), H275 (= H271), V279 (= V275), M282 (≠ I278)
- binding alpha-methyl-L-tryptophan: R64 (= R109), E66 (= E111), W155 (≠ S193), R158 (vs. gap), P160 (vs. gap), F251 (≠ H247)
5ti9D Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
43% identity, 37% coverage: 55:170/313 of query aligns to 2:128/332 of 5ti9D
- binding protoporphyrin ix containing fe: F34 (= F82), H38 (= H86), Y41 (≠ S89), L94 (= L136), S113 (= S155), G114 (= G156), F115 (= F157), F120 (≠ Y162), R121 (= R163)
- binding N'-Formylkynurenine: F34 (= F82), H38 (= H86), R106 (= R148), L109 (= L151), A112 (≠ S154), S113 (= S155), G114 (= G156)
- binding tryptophan: R65 (= R109), E67 (= E111)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 137, 286, 289, 290, 300, 301
- binding tryptophan: 170, 173, 174, 175, 253, 262, 265
Query Sequence
>H281DRAFT_04144 FitnessBrowser__Burk376:H281DRAFT_04144
MNDHMQTPGLPEEKPAQGCPFGHGRAAPPSAEAPATEGASADGWHDAQLDFSESMSYGDY
LSLGTVLDAQHPLSPDHNEMLFIIQHQTSELWMKLALYELRAALGAVHRDELPPAFKMLA
RVSRIMEQLVQAWSVLATMTPSEYTSMRPYLGSSSGFQSYQYRQIEFLLGNKNEQMLKPH
AHRAEVLAEVKASLESPSFYDEVVKLLARRGFAISPSRLTRDWTQPTVHDASVEAAWLEV
YRNPSKHWELYEMAEELVDLEDAFRQWRFRHVTTVERIIGFKQGTGGTSGAPYLRKMLDV
VLFPELWHVRTML
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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