SitesBLAST
Comparing PfGW456L13_4292 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4292 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)
73% identity, 95% coverage: 15:284/284 of query aligns to 30:299/299 of Q1LK00
- F68 (= F53) mutation to A: Abolishes catalytic activity.
- Y130 (= Y115) mutation to F: 15-fold increase in catalytic activity.
- R134 (= R119) mutation to A: Abolishes catalytic activity.
- T271 (= T256) mutation to A: Abolishes catalytic activity.
2noxB Crystal structure of tryptophan 2,3-dioxygenase from ralstonia metallidurans (see paper)
71% identity, 95% coverage: 15:284/284 of query aligns to 1:266/266 of 2noxB
- binding protoporphyrin ix containing fe: F39 (= F53), H43 (= H57), T46 (≠ S60), W90 (= W104), L93 (= L107), S112 (= S126), G113 (= G127), F114 (= F128), Y119 (= Y133), R120 (= R134), H228 (= H242), V232 (= V246), E242 (= E260), Y246 (= Y264), L247 (= L265)
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, 91% coverage: 26:284/284 of query aligns to 3:263/265 of 2nw9A
- binding 6-fluoro-l-tryptophan: F32 (= F53), H36 (= H57), Y94 (= Y115), R98 (= R119), L101 (= L122), S104 (= S125), G234 (= G255), T235 (= T256)
- binding protoporphyrin ix containing fe: F32 (= F53), H36 (= H57), S39 (= S60), W83 (= W104), L86 (= L107), G106 (= G127), F107 (= F128), Y112 (= Y133), R113 (= R134), H221 (= H242), V225 (= V246), I229 (= I250), G234 (= G255), G236 (= G257), S238 (≠ T259)
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, 93% coverage: 21:284/284 of query aligns to 17:282/298 of Q8PDA8
- FIIQH 51:55 (= FIIQH 53:57) binding
- H55 (= H57) 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 (= Y115) binding
- R117 (= R119) binding
- H240 (= H242) binding axial binding residue
- T254 (= T256) binding
7p46A Crystal structure of xanthomonas campestris tryptophan 2,3-dioxygenase (tdo) (see paper)
46% identity, 93% coverage: 21:284/284 of query aligns to 13:278/281 of 7p46A
- binding protoporphyrin ix containing fe: S51 (≠ H57), S54 (= S60), W98 (= W104), S120 (= S126), G121 (= G127), F122 (= F128), Y127 (= Y133), R128 (= R134), H236 (= H242), V240 (= V246), G249 (= G255), G251 (= G257), S253 (≠ T259)
- binding (2S)-2-amino-4-(2-aminophenyl)-4-oxobutanoic acid: F47 (= F53), S51 (≠ H57), Y109 (= Y115), R113 (= R119), S119 (= S125), G249 (= G255), T250 (= T256)
- binding tryptophan: K82 (= K88), A85 (= A91), Y216 (= Y222), S217 (≠ Q223), E220 (= E226), D224 (= D230)
1yw0A Crystal structure of the tryptophan 2,3-dioxygenase from xanthomonas campestris. Northeast structural genomics target xcr13.
43% identity, 91% coverage: 27:284/284 of query aligns to 1:241/243 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)
29% identity, 94% coverage: 4:269/284 of query aligns to 3:340/379 of P20351
- D123 (≠ E114) mutation to A: Strongly reduced enzyme activity.
- Y236 (vs. gap) mutation to F: Strongly reduced enzyme activity.
- R309 (= R239) mutation to A: Strongly reduced enzyme activity.
- H312 (= H242) binding axial binding residue
- Y335 (= Y264) mutation to F: Strongly reduced enzyme activity.
5ti9C Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
31% identity, 84% coverage: 28:266/284 of query aligns to 3:287/326 of 5ti9C
- binding protoporphyrin ix containing fe: H37 (= H57), Y40 (≠ S60), L93 (= L107), S112 (= S126), G113 (= G127), F114 (= F128), F119 (≠ Y133), R120 (= R134), W259 (= W238), H263 (= H242), V267 (= V246), M270 (≠ I249), G276 (= G255), G278 (= G257), S280 (≠ T259), L286 (= L265)
- binding N'-Formylkynurenine: F33 (= F53), H37 (= H57), R105 (= R119), L108 (= L122), A111 (≠ S125), S112 (= S126), G113 (= G127), L271 (≠ I250), G276 (= G255), T277 (= T256)
- binding tryptophan: R64 (≠ P84), E66 (≠ A86), W159 (vs. gap), R162 (vs. gap), T163 (vs. gap), P164 (vs. gap), I230 (≠ R209), F239 (≠ Y218), P242 (≠ L221)
4hkaA Crystal structure of drosophila melanogaster tryptophan 2,3- dioxygenase in complex with heme (see paper)
30% identity, 85% coverage: 28:269/284 of query aligns to 4:317/345 of 4hkaA
- binding protoporphyrin ix containing fe: H38 (= H57), Y41 (≠ S60), F45 (≠ M64), L93 (= L107), F101 (≠ Y115), F114 (= F128), Q115 (= Q129), F119 (≠ Y133), Y136 (vs. gap), W285 (= W238), H289 (= H242), V293 (= V246), Y312 (= Y264), L313 (= L265)
6pyzC Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
29% identity, 85% coverage: 25:266/284 of query aligns to 1:294/333 of 6pyzC
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y28), Y7 (= Y31), F34 (= F53), H38 (= H57), A112 (≠ S125), S113 (= S126), T284 (= T256)
- binding protoporphyrin ix containing fe: H38 (= H57), Y41 (≠ S60), L94 (= L107), G114 (= G127), F115 (= F128), F120 (≠ Y133), R121 (= R134), H270 (= H242), M273 (≠ T245), V274 (= V246), M277 (≠ I249), G283 (= G255), G285 (= G257), S287 (≠ T259), Y292 (= Y264), L293 (= L265)
- binding alpha-methyl-L-tryptophan: R65 (≠ P84), E67 (≠ A86), W167 (≠ G182), R170 (vs. gap), T171 (vs. gap), P172 (vs. gap), F246 (≠ Y218)
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)
29% identity, 84% coverage: 28:266/284 of query aligns to 42:352/406 of P48775
- Y42 (= Y28) mutation to A: Reduces enzyme activity by 99%.
- Y45 (= Y31) mutation to A: Reduces enzyme activity by 99%.
- F72 (= F53) mutation to A: Abolishes enzyme activity.
- FIITH 72:76 (≠ FIIQH 53:57) binding
- H76 (= H57) mutation to A: Abolishes enzyme activity.
- M108 (= M89) to I: in HYPTRP; reduced tryptophan 2,3-dioxygenase activity; does not affect homotetramerization; dbSNP:rs1553957997
- F140 (≠ Y115) mutation to A: Reduces enzyme activity by 99%.
- R144 (= R119) binding ; mutation to A: Reduces enzyme activity by 99%.
- S151 (= S126) mutation to A: Reduces enzyme activity by 90%.
- Y175 (vs. gap) mutation to G: Reduces enzyme activity.
- H328 (= H242) binding axial binding residue; mutation to A: Abolishes enzyme activity.
- T342 (= T256) binding
6pyzA Crystal structure of human tryptophan 2,3-dioxygenase in complex with pf-06840003 in active site (see paper)
29% identity, 85% coverage: 25:266/284 of query aligns to 1:314/353 of 6pyzA
- binding (3S)-3-(5-fluoro-1H-indol-3-yl)pyrrolidine-2,5-dione: Y4 (= Y28), Y7 (= Y31), F34 (= F53), H38 (= H57), R106 (= R119), A112 (≠ S125), S113 (= S126), T304 (= T256)
- binding protoporphyrin ix containing fe: F34 (= F53), H38 (= H57), Y41 (≠ S60), L94 (= L107), F102 (≠ Y115), S113 (= S126), G114 (= G127), F115 (= F128), F120 (≠ Y133), R121 (= R134), H290 (= H242), M293 (≠ T245), V294 (= V246), M297 (≠ I249), G303 (= G255), G305 (= G257), S307 (≠ T259), Y312 (= Y264), L313 (= L265)
- binding alpha-methyl-L-tryptophan: R65 (≠ P84), E67 (≠ A86), W170 (vs. gap), R173 (vs. gap), T174 (vs. gap), P175 (vs. gap), F266 (≠ Y218), P269 (≠ L221)
6vbnA Crystal structure of htdo2 bound to inhibitor gne1 (see paper)
29% identity, 84% coverage: 28:266/284 of query aligns to 3:313/344 of 6vbnA
- binding protoporphyrin ix containing fe: H37 (= H57), Y40 (≠ S60), L93 (= L107), F101 (≠ Y115), S112 (= S126), G113 (= G127), F114 (= F128), F119 (≠ Y133), R120 (= R134), W285 (= W238), H289 (= H242), V293 (= V246), M296 (≠ I249), L297 (≠ I250), Y311 (= Y264), L312 (= L265)
- binding 1,5-anhydro-2,3-dideoxy-3-[(5S)-5H-imidazo[5,1-a]isoindol-5-yl]-D-threo-pentitol: Y3 (= Y28), Y6 (= Y31), F33 (= F53), H37 (= H57), L108 (= L122), A111 (≠ S125), G113 (= G127)
5ti9A Crystal structure of human tdo in complex with trp and dioxygen, northeast structural genomics consortium target hr6161 (see paper)
29% identity, 85% coverage: 25:266/284 of query aligns to 1:314/350 of 5ti9A
- binding protoporphyrin ix containing fe: F34 (= F53), H38 (= H57), Y41 (≠ S60), F102 (≠ Y115), S113 (= S126), G114 (= G127), F115 (= F128), F120 (≠ Y133), R121 (= R134), W286 (= W238), H290 (= H242), M293 (≠ T245), V294 (= V246), G303 (= G255), G305 (= G257), S307 (≠ T259), L313 (= L265)
- binding tryptophan: F34 (= F53), H38 (= H57), R65 (≠ P84), E67 (≠ A86), F102 (≠ Y115), R106 (= R119), L109 (= L122), A112 (≠ S125), S113 (= S126), W170 (vs. gap), R173 (vs. gap), T174 (vs. gap), P175 (vs. gap), F266 (≠ Y218), P269 (≠ L221), G303 (= G255), T304 (= T256)
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, 88% coverage: 16:266/284 of query aligns to 29:351/403 of Q09474
- PLD 133:135 (≠ PTE 112:114) 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
31% identity, 80% coverage: 26:251/284 of query aligns to 1:248/290 of 6a4iD
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y28), Y6 (= Y31), F33 (= F53), H37 (= H57), A111 (≠ S125)
- binding protoporphyrin ix containing fe: F33 (= F53), H37 (= H57), Y40 (≠ S60), F101 (≠ Y115), S112 (= S126), G113 (= G127), F114 (= F128), F119 (≠ Y133), H239 (= H242), V243 (= V246), M246 (≠ I249)
- binding tryptophan: R64 (≠ P84), W153 (≠ A164), R156 (vs. gap), T157 (= T167), P158 (= P168), I206 (≠ R209), F215 (≠ Y218)
Sites not aligning to the query:
6a4iA Crystal structure of human tdo inhibitor complex
30% identity, 84% coverage: 28:266/284 of query aligns to 3:293/322 of 6a4iA
- binding 1-(6-chloro-1H-indazol-4-yl)cyclohexan-1-ol: Y3 (= Y28), Y6 (= Y31), F33 (= F53), H37 (= H57), A111 (≠ S125)
- binding protoporphyrin ix containing fe: F33 (= F53), H37 (= H57), Y40 (≠ S60), L93 (= L107), F101 (≠ Y115), S112 (= S126), G113 (= G127), F114 (= F128), F119 (≠ Y133), W270 (= W238), H274 (= H242), M277 (≠ T245), V278 (= V246), M281 (≠ I249), L292 (= L265)
- binding tryptophan: R64 (≠ P84), W158 (vs. gap), R161 (vs. gap), T162 (vs. gap), P163 (vs. gap), I241 (≠ R209), F250 (≠ Y218), P253 (≠ L221)
8qv7B Crystal structure of human tdo with alpha-methyl-l-tryptophan
30% identity, 80% coverage: 26:251/284 of query aligns to 1:272/310 of 8qv7B
Sites not aligning to the query:
8r5qC Structure of apo tdo with a bound inhibitor
29% identity, 80% coverage: 26:251/284 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 (= Y28), Y6 (= Y31), L7 (= L32), F33 (= F53), H37 (= H57), F101 (≠ Y115), P110 (≠ Q124), G113 (= G127), Q115 (= Q129), S116 (= S130), H273 (= H242), V277 (= V246), M280 (≠ I249)
- binding alpha-methyl-L-tryptophan: R64 (≠ P84), E66 (≠ A86), W153 (vs. gap), R156 (vs. gap), P158 (vs. gap), F249 (≠ Y218)
8r5qA Structure of apo tdo with a bound inhibitor
29% identity, 80% coverage: 26:251/284 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 (= Y28), Y6 (= Y31), L7 (= L32), F33 (= F53), H37 (= H57), F101 (≠ Y115), P110 (≠ Q124), G113 (= G127), F114 (= F128), Q115 (= Q129), S116 (= S130), H274 (= H242), V278 (= V246), M281 (≠ I249)
- binding alpha-methyl-L-tryptophan: R64 (≠ P84), E66 (≠ A86), W154 (vs. gap), R157 (vs. gap), T158 (vs. gap), P159 (vs. gap), F250 (≠ Y218)
Query Sequence
>PfGW456L13_4292 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4292
MSQCPYSPANQTEEWHNAELNFSDSMSYGDYLDLGRILSAQHPLSPDHNEMLFIIQHQTS
ELWMKLMLHELNAAREHVRLGELPPAFKMLARVSRIFDQLVHAWTVLATMTPTEYHAIRP
FLGQSSGFQSFQYREIEFILGNKSATLLRPHAHRPELLQALEKAIATPSLYDEAIRLMAS
AGLTIDPQRFERDPTSPTAHDASVEAAWRVVYTDPSRYWDLYQLAEKLIDLEDSFRQWRF
RHVTTVERIIGFQPGTGGTEGVGYLRKMLDTVLFPELWRVRSTL
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