SitesBLAST
Comparing WP_011022931.1 NCBI__GCF_000007345.1:WP_011022931.1 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)
5ey5B Lbcats
68% identity, 95% coverage: 13:396/403 of query aligns to 1:381/383 of 5ey5B
- binding pyridoxal-5'-phosphate: H81 (= H92), K82 (= K93), Q109 (= Q120), S185 (= S196), G227 (= G238), G229 (= G240), S230 (= S241), N231 (= N242), E345 (= E360), S371 (= S386), G372 (= G387)
5t6mB Structure of the tryptophan synthase b-subunit from pyroccus furiosus with b-methyltryptophan non-covalently bound (see paper)
62% identity, 96% coverage: 15:399/403 of query aligns to 3:384/386 of 5t6mB
1v8zA X-ray crystal structure of the tryptophan synthase b2 subunit from hyperthermophile, pyrococcus furiosus (see paper)
62% identity, 96% coverage: 15:399/403 of query aligns to 3:384/386 of 1v8zA
- active site: K82 (= K93), E104 (= E115), S371 (= S386)
- binding pyridoxal-5'-phosphate: H81 (= H92), K82 (= K93), Q109 (= Q120), S185 (= S196), G227 (= G238), G228 (= G239), G229 (= G240), S230 (= S241), N231 (= N242), E345 (= E360), S371 (= S386), G372 (= G387)
5dw0A Trpb from pyrococcus furiosus with l-serine bound as the external aldimine (see paper)
62% identity, 97% coverage: 15:403/403 of query aligns to 3:388/388 of 5dw0A
- active site: K82 (= K93), E104 (= E115), S371 (= S386)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine: H81 (= H92), K82 (= K93), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G227 (= G238), G229 (= G240), S230 (= S241), N231 (= N242), G298 (= G313), D300 (= D315), E345 (= E360), S371 (= S386)
6am8B Engineered tryptophan synthase b-subunit from pyrococcus furiosus, pftrpb2b9 with trp bound as e(aex2) (see paper)
63% identity, 95% coverage: 15:397/403 of query aligns to 3:382/385 of 6am8B
- active site: K82 (= K93), E104 (= E115), S371 (= S386)
- binding [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-l-tryptophane: H81 (= H92), K82 (= K93), E104 (= E115), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), L161 (= L172), S185 (= S196), V187 (= V198), G227 (= G238), G228 (= G239), G229 (= G240), S230 (= S241), N231 (= N242), G298 (= G313), Y301 (= Y316), E345 (= E360), S371 (= S386), G372 (= G387)
- binding tryptophan: P12 (= P24), L169 (≠ M180), S274 (≠ L289), H275 (= H290)
5dw3A Tryptophan synthase beta-subunit from pyrococcus furiosus with product l-tryptophan non-covalently bound in the active site (see paper)
62% identity, 96% coverage: 15:399/403 of query aligns to 3:383/383 of 5dw3A
- active site: K82 (= K93), E104 (= E115), S370 (= S386)
- binding tryptophan: K82 (= K93), E104 (= E115), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G228 (= G239), Y300 (= Y316)
5t6mA Structure of the tryptophan synthase b-subunit from pyroccus furiosus with b-methyltryptophan non-covalently bound (see paper)
62% identity, 96% coverage: 15:399/403 of query aligns to 3:382/383 of 5t6mA
5ixjD Tryptophan synthase beta-subunit from pyrococcus furiosus with l- threonine non-covalently bound in the active site (see paper)
62% identity, 97% coverage: 15:403/403 of query aligns to 3:386/394 of 5ixjD
7rnpA Engineered tryptophan synthase b-subunit from pyrococcus furiosus, pftrpb2b9_h275e with 4-cl-trp non-covalently bound (see paper)
63% identity, 95% coverage: 15:397/403 of query aligns to 3:382/384 of 7rnpA
5vm5D Engineered tryptophan synthase b-subunit from pyrococcus furiosus, pftrpb2b9, with ser bound (see paper)
63% identity, 95% coverage: 15:397/403 of query aligns to 3:380/383 of 5vm5D
- active site: K82 (= K93), E104 (= E115), S369 (= S386)
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: H81 (= H92), K82 (= K93), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G227 (= G238), G229 (= G240), S230 (= S241), N231 (= N242), G296 (= G313), E343 (= E360), S369 (= S386)
6cuzA Engineered trpb from pyrococcus furiosus, pftrpb7e6 with (2s,3r)- ethylserine bound as the amino-acrylate (see paper)
62% identity, 95% coverage: 15:397/403 of query aligns to 3:382/383 of 6cuzA
- binding (2E)-2-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]pent-2-enoic acid: H81 (= H92), K82 (= K93), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G227 (= G238), G229 (= G240), S230 (= S241), N231 (= N242), G298 (= G313), E345 (= E360), S371 (= S386)
6cutA Engineered holo trpb from pyrococcus furiosus, pftrpb7e6 with (2s,3s)- isopropylserine bound as the external aldimine (see paper)
62% identity, 95% coverage: 15:397/403 of query aligns to 3:382/385 of 6cutA
- binding (2S,3S)-3-hydroxy-2-[(E)-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)amino]-4-methylpentanoic acid (non-preferred name): H81 (= H92), K82 (= K93), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G227 (= G238), G229 (= G240), S230 (= S241), N231 (= N242), G298 (= G313), E345 (= E360), S371 (= S386)
8egzB Engineered tyrosine synthase (tmtyrs1) derived from t. Maritima trpb with ser bound as the amino-acrylate intermediate
64% identity, 96% coverage: 12:398/403 of query aligns to 1:379/386 of 8egzB
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: H81 (= H92), K82 (= K93), T105 (= T116), G106 (= G117), A107 (= A118), Q109 (= Q120), H110 (= H121), S185 (= S196), G229 (= G240), S230 (= S241), N231 (= N242), G297 (= G313), E344 (= E360), S367 (= S386)
8eh1A Engineered tyrosine synthase (tmtyrs1) derived from t. Maritima trpb with ser bound as the amino-acrylate intermediate and complexed with 4-hydroxyquinoline
64% identity, 96% coverage: 13:398/403 of query aligns to 1:378/383 of 8eh1A
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: H80 (= H92), K81 (= K93), T104 (= T116), G105 (= G117), A106 (= A118), Q108 (= Q120), H109 (= H121), S184 (= S196), G228 (= G240), S229 (= S241), N230 (= N242), G296 (= G313), E343 (= E360), S366 (= S386)
- binding quinolin-4-ol: G103 (≠ E115), L160 (= L172), I164 (= I176), G183 (= G195), S184 (= S196), Y299 (= Y316)
8eh0A Engineered tyrosine synthase (tmtyrs1) derived from t. Maritima trpb with ser bound as the amino-acrylate intermediate and complexed with quinoline n-oxide
64% identity, 96% coverage: 13:398/403 of query aligns to 1:378/385 of 8eh0A
- binding 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid: H80 (= H92), K81 (= K93), T104 (= T116), G105 (= G117), A106 (= A118), Q108 (= Q120), H109 (= H121), S184 (= S196), G228 (= G240), S229 (= S241), N230 (= N242), G296 (= G313), E343 (= E360), S366 (= S386), G367 (= G387)
- binding 1-oxo-1lambda~5~-quinoline: L160 (= L172), I164 (= I176), Y180 (= Y192), P182 (≠ I194), G183 (= G195), S184 (= S196), V186 (= V198), Y299 (= Y316)
8egyA Engineered holo tyrosine synthase (tmtyrs1) derived from t. Maritima trpb
64% identity, 96% coverage: 13:398/403 of query aligns to 1:378/385 of 8egyA
5tciH Crystal structure of tryptophan synthase from m. Tuberculosis - brd4592-bound form (see paper)
55% identity, 94% coverage: 18:395/403 of query aligns to 22:396/406 of 5tciH
- active site: K98 (= K93), E120 (= E115), S387 (= S386)
- binding (2R,3S,4R)-3-(2'-fluoro[1,1'-biphenyl]-4-yl)-4-(hydroxymethyl)azetidine-2-carbonitrile: P28 (= P24), L31 (= L27), Y197 (= Y192), F199 (≠ I194), P205 (= P200), F208 (≠ Y203), H291 (= H290)
6uapB Crystal structure of tryptophan synthase from m. Tuberculosis - open form with brd6309 bound
55% identity, 94% coverage: 18:395/403 of query aligns to 21:395/405 of 6uapB
- active site: K97 (= K93), E119 (= E115), S386 (= S386)
- binding (2R,3S,4R)-3-(4'-chloro-2',6'-difluoro[1,1'-biphenyl]-4-yl)-4-(fluoromethyl)azetidine-2-carbonitrile: I180 (= I176), N181 (= N177), F184 (≠ M180), Y196 (= Y192), F198 (≠ I194), P204 (= P200), F207 (≠ Y203), H290 (= H290)
6u6cB Crystal structure of tryptophan synthase from m. Tuberculosis - aminoacrylate- and gsk2-bound form (see paper)
55% identity, 94% coverage: 18:395/403 of query aligns to 22:396/405 of 6u6cB
- active site: K98 (= K93), E120 (= E115), S387 (= S386)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: H97 (= H92), K98 (= K93), T121 (= T116), G122 (= G117), A123 (= A118), Q125 (= Q120), H126 (= H121), T201 (≠ S196), G243 (= G238), G245 (= G240), S246 (= S241), N247 (= N242), G314 (= G313), E361 (= E360), S387 (= S386)
- binding 1-(2-fluorobenzene-1-carbonyl)-N-methyl-2,3-dihydro-1H-indole-5-sulfonamide: Y26 (= Y22), F185 (≠ M180), W188 (= W183), Y197 (= Y192), F199 (≠ I194), G204 (= G199), P205 (= P200), H291 (= H290), G292 (= G291)
5ocwB Structure of mycobacterium tuberculosis tryptophan synthase in space group f222 (see paper)
55% identity, 94% coverage: 18:395/403 of query aligns to 17:391/399 of 5ocwB
- active site: K93 (= K93), E115 (= E115), S382 (= S386)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: H92 (= H92), K93 (= K93), T116 (= T116), G117 (= G117), A118 (= A118), Q120 (= Q120), H121 (= H121), T196 (≠ S196), G238 (= G238), G240 (= G240), S241 (= S241), N242 (= N242), G309 (= G313), E356 (= E360), S382 (= S386)
Query Sequence
>WP_011022931.1 NCBI__GCF_000007345.1:WP_011022931.1
MTETKVSEFQLKGKYGKYGGQYVPEVLMPALEELDVGYEKYKNDPESLAELDHYLRDFAG
RETPLYFARNLSKKYGTKVYLKREDLVHGGAHKLNNALGQALLAKFMGKTRLIAETGAGQ
HGTATAMVGATLGFETIVYMGAKDIKRQQMNAYRMELMGTEVRAVETGSKTLKDAINEAM
RDWVTNIENTHYLIGSVVGPHPYPMIVRDFQSVIGKEVKEQAMEKEGRLPDSIIACAGGG
SNAMGTFHPFIEDREVKLIAVEAGGKGLKCTEKAALHSASLCIGEEGILHGARTKILQDK
NGQILESESVSAGLDYSGVGPELAYLSESGRVTARYVTDDEALDAFNELSRLEGIIPALE
SSHALAYLKKAAESGELGEFVVVNLSGRGDKDLETVLSLRRGV
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