SitesBLAST
Comparing 352706 FitnessBrowser__Btheta:352706 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)
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
80% identity, 97% coverage: 31:1024/1024 of query aligns to 2:996/1003 of 3bgaA
- active site: D201 (= D229), H354 (= H382), H387 (= H415), E412 (= E440), H414 (= H442), E458 (= E486), Y499 (= Y527), E522 (= E550), S584 (= S612), F588 (= F616), N591 (= N619)
- binding magnesium ion: E412 (= E440), H414 (= H442), E458 (= E486)
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
40% identity, 94% coverage: 32:995/1024 of query aligns to 3:953/1083 of 6s6zA
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
32% identity, 97% coverage: 33:1024/1024 of query aligns to 4:1001/1030 of P06864
- E449 (= E486) active site, Proton donor
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
33% identity, 94% coverage: 29:995/1024 of query aligns to 13:995/1024 of P00722
- D202 (= D229) mutation D->E,N: Causes a significant decrease in binding affinity in the absence of monovalent cations or in the presence of potassium ions, but only a moderate decrease in the presence of sodium ions.; mutation to F: Obliterates all binding and catalysis.
- H358 (= H382) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H415) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E440) binding
- H419 (= H442) binding
- E462 (= E486) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E550) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H553) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ S612) binding
- F602 (= F616) mutation to A: Decreases the stability of the loop 794-804.
- G795 (≠ R798) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ M801) mutation E->A,L: The catalytic efficiency is not increased, when the sodium concentration increases.; mutation E->D,Q: Small increase of the catalytic efficiency, when the sodium concentration increases.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 1000 mutation W->F,G,L,T: Decreases affinity for substrate.
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 11:993/1022 of 5a1aA
- active site: D200 (= D229), H356 (= H382), H390 (= H415), E415 (= E440), H417 (= H442), E460 (= E486), Y502 (= Y527), E536 (= E550), N596 (≠ S612), F600 (= F616), N603 (= N619)
- binding magnesium ion: D14 (≠ E32), W15 (= W33), N17 (≠ S35), V20 (≠ A38), Q162 (= Q191), D192 (≠ S221), E415 (= E440), H417 (= H442), E460 (= E486)
- binding sodium ion: D200 (= D229), H539 (= H553), F555 (= F569), Y558 (≠ E572), P559 (= P573), L561 (≠ A575), F600 (= F616), N603 (= N619)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N123), D200 (= D229), M501 (= M526), Y502 (= Y527), H539 (= H553), D597 (≠ F613), F600 (= F616)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 12:994/1023 of 7btkC
- binding 4-[[2-[(E)-2-[4-[(2S,3R,4S,5R,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]ethenyl]-3,3-dimethyl-2H-indol-1-yl]methyl]benzoic acid: N102 (= N123), D201 (= D229), H391 (= H415), N460 (= N485), E461 (= E486), Y503 (= Y527), F512 (vs. gap), Q537 (≠ E550), W568 (= W581)
- binding magnesium ion: D15 (≠ E32), N18 (≠ S35), V21 (≠ A38), Q163 (= Q191), D193 (≠ S221), D201 (= D229), E416 (= E440), H418 (= H442), E461 (= E486)
Sites not aligning to the query:
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 10:992/1021 of 7brsA
- binding 8-[2-[(E)-2-[4-[(2S,3R,4S,5R,6R)-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]ethenyl]-3,3-dimethyl-indol-1-ium-1-yl]octanoic acid: N100 (= N123), D199 (= D229), E459 (= E486), Y501 (= Y527), Q535 (≠ E550), H538 (= H553), N602 (= N619)
- binding magnesium ion: D13 (≠ E32), N16 (≠ S35), V19 (≠ A38), Q161 (= Q191), D191 (≠ S221), E414 (= E440), H416 (= H442), E459 (= E486)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 10:992/1021 of 6kuzA
- binding 3-(1,3-benzothiazol-2-yl)-2-[[4-[(2~{S},3~{R},4~{S},5~{R},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxyphenyl]methoxy]-5-methyl-benzaldehyde: N100 (= N123), D199 (= D229), H389 (= H415), H416 (= H442), E459 (= E486), Y501 (= Y527), Q535 (≠ E550), H538 (= H553), W566 (= W581)
- binding magnesium ion: D13 (≠ E32), N16 (≠ S35), V19 (≠ A38), Q161 (= Q191), D191 (≠ S221), E414 (= E440), H416 (= H442), E459 (= E486)
Sites not aligning to the query:
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 4:986/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D229), H383 (= H415), E453 (= E486), E529 (= E550), H532 (= H553), W560 (= W581), F593 (= F616)
- binding magnesium ion: E408 (= E440), H410 (= H442), E453 (= E486)
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jz6A
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), E525 (= E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D229), H379 (= H415), E449 (= E486), Y491 (= Y527), E525 (= E550), H528 (= H553), W556 (= W581), N592 (= N619)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486), S635 (≠ L665), E638 (≠ Y668), L658 (≠ V689)
- binding sodium ion: D189 (= D229), F544 (= F569), Y547 (≠ E572), P548 (= P573), L550 (≠ A575), F589 (= F616), C590 (= C617), N592 (= N619), F919 (≠ I925), P920 (= P926), L955 (= L968), M956 (≠ E969), T958 (≠ A971)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jz5A
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), E525 (= E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding D-galactonolactone: D189 (= D229), H379 (= H415), N448 (= N485), E449 (= E486), M490 (= M526), Y491 (= Y527), E525 (= E550), H528 (= H553), W556 (= W581), F589 (= F616), N592 (= N619)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jz3A
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), E525 (= E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D229), H379 (= H415), E449 (= E486), Y491 (= Y527), E525 (= E550), H528 (= H553), W556 (= W581), F589 (= F616)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jz2A
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), E525 (= E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D229), H379 (= H415), N448 (= N485), E449 (= E486), Y491 (= Y527), E525 (= E550), H528 (= H553), W556 (= W581), F589 (= F616)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
- binding sodium ion: D189 (= D229), F544 (= F569), Y547 (≠ E572), P548 (= P573), L550 (≠ A575), Q551 (= Q576), F589 (= F616), N592 (= N619), F919 (≠ I925), P920 (= P926), L955 (= L968), M956 (≠ E969), T958 (≠ A971)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jyxA
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), E525 (= E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N123), D189 (= D229), E292 (= E329), P294 (= P331), E449 (= E486), E525 (= E550), H528 (= H553), N592 (= N619), R633 (≠ S663), D636 (≠ N666), Q690 (≠ R721), W696 (≠ L727)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
- binding sodium ion: D189 (= D229), F544 (= F569), Y547 (≠ E572), P548 (= P573), L550 (≠ A575), Q551 (= Q576), F589 (= F616), C590 (= C617), N592 (= N619), F919 (≠ I925), P920 (= P926), L955 (= L968), M956 (≠ E969), T958 (≠ A971)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
33% identity, 94% coverage: 29:995/1024 of query aligns to 4:986/1015 of 4duxA
- active site: D193 (= D229), H349 (= H382), H383 (= H415), E408 (= E440), H410 (= H442), E453 (= E486), Y495 (= Y527), E529 (= E550), N589 (≠ S612), F593 (= F616), N596 (= N619)
- binding beta-L-ribopyranose: D193 (= D229), H383 (= H415), E453 (= E486), M494 (= M526), Y495 (= Y527), E529 (= E550), H532 (= H553), W560 (= W581), F593 (= F616), S788 (≠ R800)
- binding magnesium ion: D7 (≠ E32), N10 (≠ S35), V13 (≠ A38), Q155 (= Q191), D185 (≠ S221), E408 (= E440), H410 (= H442), E453 (= E486)
Sites not aligning to the query:
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jywA
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), Q525 (≠ E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N123), D189 (= D229), E449 (= E486), Y491 (= Y527), Q525 (≠ E550), H528 (= H553), N592 (= N619)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jyvA
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), Q525 (≠ E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N123), N90 (= N123), V91 (≠ E124), D189 (= D229), H406 (= H442), E449 (= E486), Y491 (= Y527), H528 (= H553), D586 (≠ F613), F589 (= F616), N592 (= N619), V783 (≠ D799), V783 (≠ D799), E785 (≠ M801), R788 (≠ K804)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
33% identity, 94% coverage: 32:995/1024 of query aligns to 3:982/1011 of 1jynA
- active site: D189 (= D229), H345 (= H382), H379 (= H415), E404 (= E440), H406 (= H442), E449 (= E486), Y491 (= Y527), Q525 (≠ E550), N585 (≠ S612), F589 (= F616), N592 (= N619)
- binding beta-D-glucopyranose: N90 (= N123)
- binding beta-D-galactopyranose: N90 (= N123), D189 (= D229), E449 (= E486), Y491 (= Y527), H528 (= H553), N592 (= N619)
- binding magnesium ion: D3 (≠ E32), N6 (≠ S35), V9 (≠ A38), Q151 (= Q191), D181 (≠ S221), E404 (= E440), H406 (= H442), E449 (= E486)
- binding sodium ion: D189 (= D229), F544 (= F569), Y547 (≠ E572), P548 (= P573), L550 (≠ A575), F589 (= F616), N592 (= N619), S635 (≠ L665), D636 (≠ N666), E638 (≠ Y668), L658 (≠ V689), F919 (≠ I925), P920 (= P926), L955 (= L968), M956 (≠ E969), T958 (≠ A971)
Sites not aligning to the query:
6sebA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cb in complex with iptg (see paper)
34% identity, 93% coverage: 71:1020/1024 of query aligns to 37:985/989 of 6sebA
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: D186 (= D229), E420 (= E486), Y461 (= Y527), E496 (= E550), H499 (= H553), D887 (≠ F920), R939 (≠ I974), L942 (= L977), K943 (≠ E978), A944 (≠ R979), C964 (= C999)
6secA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cbon complex with onpg (see paper)
34% identity, 93% coverage: 71:1020/1024 of query aligns to 37:985/988 of 6secA
Query Sequence
>352706 FitnessBrowser__Btheta:352706
MIKMNNLLKPFFLMMLAAPAIISTTAQQQQPEWQSQYAVGLNKLDPHTYVWPYADASEVE
KGTFEQSPYYMSLNGQWKFHWVKNPDTRPKDFYKPSYYTGGWADIKVPGNWERQGYGTAI
YVNETYEFDDKMFNFKKNPPLVPYKENEVGSYRRTFKVPAGWEGRRVVLCCEGVISFYYV
WVNGEFLGYNQGSKTAAEWDITDKLTDGENTIALEVYRWSSGAYLECQDMWRLSGIERDV
YLYSTPEQYIADYKVTSLLEKEHYKEGIFELEVAVGGTASGTSSIAYTLKDASDKTVLEG
SRKLESHGSGNLIVFDEQRLPDVRRWNAEHPELYTLLLELKDAGGKVTEITGTKVGFRTS
EIKNGRFCINGVPVLVKGVNRHEHSQLGRTVSKELMEQDIRLMKQHNINTVRNSHYPAHP
YWYQLCDRYGLYVIDEANIESHGMGYGPASLAKDSTWLPAHIDRTRRMYERSKNHPSVVI
WSLGNEAGNGINFERTYDWLKSVEKNRPVQYERAEENYNTDIYCRMYRSVDVIRNYVARK
DIYRPFILCEYLHAMGNSCGGMKEYWEVFENEPMAQGGCIWDWVDQSFREVDKDGKWYWT
YGGDYGPKDVPSFGNFCCNGLVNAVREPHPHLLEVKKIYQNIKSTLIDKKNLTVRVKNWF
DFSDLNEYILHWKVTGDDGTVLAEGNKEVACEPHATVELTLGAVQLPKTIREAYLDLGWT
RKKSTPLVDTAWEIAYDQFVLPASGKVWNGKPSEAGKTTFEVDENTGALKSLCLDGEELL
ASPVTISLFRPATDNDNRDRMGAKLWRKAGLHTLTQKVVSLKESKTSATAQVNILNVTGK
KVGDATLEYTLNHNGSLKVQTTFQPDTTWVKSIARLGLTFEMNDTYGNVTYLGRGEHETY
IDRNQSGKIGIYTTTPEKMFHYYVIPQSTGNRTDVRWVKLADDSGKGCWIESDSPFQFSA
LPFSDLLLEKALHINDLERNGRITVHLDAKQAGVGTATCGPGVLPPYLVPLGKQTFTFTI
YPVK
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