SitesBLAST
Comparing 352820 FitnessBrowser__Btheta:352820 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
38% identity, 71% coverage: 29:1042/1421 of query aligns to 3:977/1083 of 6s6zA
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
34% identity, 72% coverage: 28:1051/1421 of query aligns to 2:999/1003 of 3bgaA
- active site: D201 (= D241), H354 (= H387), H387 (= H421), E412 (= E446), H414 (= H448), E458 (= E488), Y499 (= Y527), E522 (= E557), S584 (≠ N618), F588 (= F622), N591 (= N625)
- binding magnesium ion: E412 (= E446), H414 (= H448), E458 (= E488)
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
32% identity, 72% coverage: 30:1055/1421 of query aligns to 4:1008/1030 of P06864
- E449 (= E488) 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, 70% coverage: 11:1000/1421 of query aligns to 1:981/1024 of P00722
- M1 (≠ I11) modified: Initiator methionine, Removed
- D202 (= D241) 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 (= H387) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H421) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E446) binding
- H419 (= H448) binding
- E462 (= E488) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E557) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H560) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (= N618) binding
- F602 (= F622) mutation to A: Decreases the stability of the loop 794-804.
- G795 (vs. gap) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (vs. gap) 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:
- 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, 69% coverage: 17:1000/1421 of query aligns to 5:979/1022 of 5a1aA
- active site: D200 (= D241), H356 (= H387), H390 (= H421), E415 (= E446), H417 (= H448), E460 (= E488), Y502 (= Y527), E536 (= E557), N596 (= N618), F600 (= F622), N603 (= N625)
- binding magnesium ion: D14 (= D26), W15 (= W30), N17 (= N32), V20 (= V35), Q162 (≠ E203), D192 (= D233), E415 (= E446), H417 (= H448), E460 (= E488)
- binding sodium ion: D200 (= D241), H539 (= H560), F555 (≠ Y576), Y558 (= Y579), P559 (= P580), L561 (= L582), F600 (= F622), N603 (= N625)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N126), D200 (= D241), M501 (= M526), Y502 (= Y527), H539 (= H560), D597 (= D619), F600 (= F622)
Sites not aligning to the query:
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
33% identity, 69% coverage: 17:1000/1421 of query aligns to 4:978/1021 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 (= N126), D199 (= D241), E459 (= E488), Y501 (= Y527), Q535 (≠ E557), H538 (= H560), N602 (= N625)
- binding magnesium ion: D13 (= D26), N16 (= N32), V19 (= V35), Q161 (≠ E203), D191 (= D233), E414 (= E446), H416 (= H448), E459 (= E488)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
33% identity, 69% coverage: 17:1000/1421 of query aligns to 4:978/1021 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 (= N126), D199 (= D241), H389 (= H421), H416 (= H448), E459 (= E488), Y501 (= Y527), Q535 (≠ E557), H538 (= H560), W566 (= W588)
- binding magnesium ion: D13 (= D26), N16 (= N32), V19 (= V35), Q161 (≠ E203), D191 (= D233), E414 (= E446), H416 (= H448), E459 (= E488)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
33% identity, 69% coverage: 17:1000/1421 of query aligns to 6:980/1023 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 (= N126), D201 (= D241), H391 (= H421), N460 (= N487), E461 (= E488), Y503 (= Y527), F512 (≠ L533), Q537 (≠ E557), W568 (= W588)
- binding magnesium ion: D15 (= D26), N18 (= N32), V21 (= V35), Q163 (≠ E203), D193 (= D233), D201 (= D241), E416 (= E446), H418 (= H448), E461 (= E488)
Sites not aligning to the query:
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jz6A
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), E525 (= E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D241), H379 (= H421), E449 (= E488), Y491 (= Y527), E525 (= E557), H528 (= H560), W556 (= W588), N592 (= N625)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488), S635 (≠ L669), E638 (≠ L672), L658 (= L693)
- binding sodium ion: D189 (= D241), F544 (≠ Y576), Y547 (= Y579), P548 (= P580), L550 (= L582), F589 (= F622), C590 (= C623), N592 (= N625), F919 (≠ R943), P920 (≠ A944), L955 (= L979), M956 (≠ H980), T958 (= T982)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jz5A
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), E525 (= E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding D-galactonolactone: D189 (= D241), H379 (= H421), N448 (= N487), E449 (= E488), M490 (= M526), Y491 (= Y527), E525 (= E557), H528 (= H560), W556 (= W588), F589 (= F622), N592 (= N625)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jz3A
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), E525 (= E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D241), H379 (= H421), E449 (= E488), Y491 (= Y527), E525 (= E557), H528 (= H560), W556 (= W588), F589 (= F622)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jz2A
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), E525 (= E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D241), H379 (= H421), N448 (= N487), E449 (= E488), Y491 (= Y527), E525 (= E557), H528 (= H560), W556 (= W588), F589 (= F622)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
- binding sodium ion: D189 (= D241), F544 (≠ Y576), Y547 (= Y579), P548 (= P580), L550 (= L582), Q551 (≠ V583), F589 (= F622), N592 (= N625), F919 (≠ R943), P920 (≠ A944), L955 (= L979), M956 (≠ H980), T958 (= T982)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jyxA
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), E525 (= E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N126), D189 (= D241), E292 (= E334), P294 (= P336), E449 (= E488), E525 (= E557), H528 (= H560), N592 (= N625), R633 (≠ A667), D636 (= D670), Q690 (= Q726), W696 (= W732)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
- binding sodium ion: D189 (= D241), F544 (≠ Y576), Y547 (= Y579), P548 (= P580), L550 (= L582), Q551 (≠ V583), F589 (= F622), C590 (= C623), N592 (= N625), F919 (≠ R943), P920 (≠ A944), L955 (= L979), M956 (≠ H980), T958 (= T982)
Sites not aligning to the query:
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 7:972/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D241), H383 (= H421), E453 (= E488), E529 (= E557), H532 (= H560), W560 (= W588), F593 (= F622)
- binding magnesium ion: E408 (= E446), H410 (= H448), E453 (= E488)
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jywA
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), Q525 (≠ E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N126), D189 (= D241), E449 (= E488), Y491 (= Y527), Q525 (≠ E557), H528 (= H560), N592 (= N625)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jyvA
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), Q525 (≠ E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N126), N90 (= N126), V91 (= V127), D189 (= D241), H406 (= H448), E449 (= E488), Y491 (= Y527), H528 (= H560), D586 (= D619), F589 (= F622), N592 (= N625), V783 (vs. gap), V783 (vs. gap), E785 (vs. gap), R788 (≠ Q817)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 3:968/1011 of 1jynA
- active site: D189 (= D241), H345 (= H387), H379 (= H421), E404 (= E446), H406 (= H448), E449 (= E488), Y491 (= Y527), Q525 (≠ E557), N585 (= N618), F589 (= F622), N592 (= N625)
- binding beta-D-glucopyranose: N90 (= N126)
- binding beta-D-galactopyranose: N90 (= N126), D189 (= D241), E449 (= E488), Y491 (= Y527), H528 (= H560), N592 (= N625)
- binding magnesium ion: D3 (≠ E29), N6 (= N32), V9 (= V35), Q151 (≠ E203), D181 (= D233), E404 (= E446), H406 (= H448), E449 (= E488)
- binding sodium ion: D189 (= D241), F544 (≠ Y576), Y547 (= Y579), P548 (= P580), L550 (= L582), F589 (= F622), N592 (= N625), S635 (≠ L669), D636 (= D670), E638 (≠ L672), L658 (= L693), F919 (≠ R943), P920 (≠ A944), L955 (= L979), M956 (≠ H980), T958 (= T982)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
33% identity, 68% coverage: 29:1000/1421 of query aligns to 7:972/1015 of 4duxA
- active site: D193 (= D241), H349 (= H387), H383 (= H421), E408 (= E446), H410 (= H448), E453 (= E488), Y495 (= Y527), E529 (= E557), N589 (= N618), F593 (= F622), N596 (= N625)
- binding beta-L-ribopyranose: D193 (= D241), H383 (= H421), E453 (= E488), M494 (= M526), Y495 (= Y527), E529 (= E557), H532 (= H560), W560 (= W588), F593 (= F622), S788 (vs. gap)
- binding magnesium ion: D7 (≠ E29), N10 (= N32), V13 (= V35), Q155 (≠ E203), D185 (= D233), E408 (= E446), H410 (= H448), E453 (= E488)
Sites not aligning to the query:
1yq2A Beta-galactosidase from arthrobacter sp. C2-2 (isoenzyme c2-2-1) (see paper)
32% identity, 69% coverage: 69:1046/1421 of query aligns to 31:1019/1020 of 1yq2A
- active site: D198 (= D241), H332 (= H387), H366 (= H421), E391 (= E446), H393 (= H448), E439 (= E488), Y480 (= Y527), E518 (= E557), H578 (≠ N618), F582 (= F622), D585 (≠ N625)
- binding magnesium ion: A522 (= A561), G524 (= G563), G526 (≠ S565)
6sebA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cb in complex with iptg (see paper)
30% identity, 69% coverage: 69:1044/1421 of query aligns to 38:985/989 of 6sebA
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: D186 (= D241), E420 (= E488), Y461 (= Y527), E496 (= E557), H499 (= H560), D887 (≠ W938), R939 (= R993), L942 (≠ V1001), K943 (≠ P1002), A944 (≠ M1003), C964 (= C1023)
Query Sequence
>352820 FitnessBrowser__Btheta:352820
MKLRIMRSAWIALLFMSLSVTAQTTDKPEWSNELVSGVNKEEAVQIAIPFTDEQQAMNLT
IEESPYYKTLNGIWKFHWVADPKDRPQDFCKPEYDVSQWDNIKVPATWQIEAVRHNKNWD
KPLYCNVIYPFCEWDWKKIQWPNVIQPRPSNYTFATMPNPVGSYRREFILPDSWKGRDIF
IRFNGVEAGFYIWVNGKKVGYSEDSYLPAEFNLTPYLKAGKNVLAVEVYRFTDGSFLECQ
DFWRFSGIFRDVFLWSAPKTQIRDFFFRTDLDKEYKNASVSLDIDITGKRSNNEIQVKVT
DQNGKEIATQNARAVTGTNKLQFEVVNPLKWTAETPNLYNLTILLKQKGKTVDIRSVKVG
FRKIELAQDGRLLINGKSTLFKGVDRHDHSSENGRTVSKEEMEKDVQLMKSLNINAVRTS
HYPNNPYFYDLCDRYGIYVLSEANVECHGLMALSSEPSWVKAFTERSENMVRRYKNHASI
VMWSLGNESGNGINFKSAAEAVKKLDDTRPTHYEGNSSYCDVTSSMYPDVQWLESVGKER
LQKFQNGETVKPHVVCEYAHAMGNSIGNFKEYWETYERYPALVGGFIWDWVDQSIKMPAP
DGSGYYMAFGGDFGDTPNDGNFCTNGVIFSDRTYSAKAYEVKKIHQPVWVEAMGNGTYKL
TNKRFHAGLDDLYGRYEIEEDGKVVFSANLEELSLNAQDSKVITIADNQINKIPGAEYFI
KFRFCQKQDTEWEKAGYEVASEQFKLSDSAKPVFKAGEGSIDLIETDDAYLVKGSQFEAS
FSKQQGTISSYTLNELPMISKGLELNAFRAPTDNDKQVDGDWYQKGLYQMTLEPGHWNVR
KEDNKVTLQIENLYRGKTGFDYRTNIEYTVAADGSILVNSTIIPSTKGVIIPRIGYRMEL
PEGFERMRWYGRGPLENYVDRKDATYVGVYDELVSDQWVNYVRAQEMGNREDLRWISITN
PDGIGFVFIAGDKMSASALHATAQDMVDPANHRRLLHKYEVPMRKETVLCLDANQRPLGN
ASCGPGPMQKYELRSQPTVFSFIILPLERSYSTEELIKKARVQMPVCMPVLIERDNNGYL
NLKTNTPGATVHYSLNGGEEKIYTEPFEFISGGHVEAYAVSEQLGKSARTSAEFPIYVDR
SLWKIVSVSSENGGEEARNAIDGDLNTIWHSRWNDPVAKHPHEIVVDMSSSLEIDKFIYQ
PRNSENGRIKDYELYFSKDGKNWENKTKGRFENSSSAQFVTLEKPIVARYFKLIALSEIY
GRDWASAAELNVNAVRNLSGASEERQKVVYADSDADGSMKLAADGDINTFWHTVHNQFYL
APYPHEIQIALAKETTVKGLKYTPRQDSSEGRIGKYEVYISHDGKEWGKAVASGTFADSK
EVQTVEFNPCKARYVKLQALSAVIKEAKMAAVAELEVLLAE
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