SitesBLAST
Comparing 351154 FitnessBrowser__Btheta:351154 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)
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
100% identity, 97% coverage: 27:1022/1022 of query aligns to 1:996/1003 of 3bgaA
- active site: D201 (= D227), H354 (= H380), H387 (= H413), E412 (= E438), H414 (= H440), E458 (= E484), Y499 (= Y525), E522 (= E548), S584 (= S610), F588 (= F614), N591 (= N617)
- binding magnesium ion: E412 (= E438), H414 (= H440), E458 (= E484)
6s6zA Structure of beta-galactosidase from thermotoga maritima (see paper)
39% identity, 97% coverage: 29:1018/1022 of query aligns to 3:979/1083 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: 30:1022/1022 of query aligns to 4:1001/1030 of P06864
- E449 (= E484) active site, Proton donor
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jz6A
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), E525 (= E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D227), H379 (= H413), E449 (= E484), Y491 (= Y525), E525 (= E548), H528 (= H551), W556 (= W579), N592 (= N617)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484), S635 (≠ L663), E638 (≠ Y666), L658 (≠ V687)
- binding sodium ion: D189 (= D227), F544 (= F567), Y547 (≠ E570), P548 (= P571), L550 (≠ A573), F589 (= F614), C590 (= C615), N592 (= N617), F919 (≠ T923), P920 (= P924), L955 (= L966), M956 (≠ E967), T958 (≠ A969)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jz5A
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), E525 (= E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding D-galactonolactone: D189 (= D227), H379 (= H413), N448 (= N483), E449 (= E484), M490 (= M524), Y491 (= Y525), E525 (= E548), H528 (= H551), W556 (= W579), F589 (= F614), N592 (= N617)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jz3A
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), E525 (= E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D227), H379 (= H413), E449 (= E484), Y491 (= Y525), E525 (= E548), H528 (= H551), W556 (= W579), F589 (= F614)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jz2A
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), E525 (= E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D227), H379 (= H413), N448 (= N483), E449 (= E484), Y491 (= Y525), E525 (= E548), H528 (= H551), W556 (= W579), F589 (= F614)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
- binding sodium ion: D189 (= D227), F544 (= F567), Y547 (≠ E570), P548 (= P571), L550 (≠ A573), Q551 (= Q574), F589 (= F614), N592 (= N617), F919 (≠ T923), P920 (= P924), L955 (= L966), M956 (≠ E967), T958 (≠ A969)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jyxA
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), E525 (= E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (= N121), D189 (= D227), E292 (= E327), P294 (= P329), E449 (= E484), E525 (= E548), H528 (= H551), N592 (= N617), R633 (≠ S661), D636 (≠ N664), Q690 (≠ R719), W696 (≠ L725)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
- binding sodium ion: D189 (= D227), F544 (= F567), Y547 (≠ E570), P548 (= P571), L550 (≠ A573), Q551 (= Q574), F589 (= F614), C590 (= C615), N592 (= N617), F919 (≠ T923), P920 (= P924), L955 (= L966), M956 (≠ E967), T958 (≠ A969)
Sites not aligning to the query:
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 7:986/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D227), H383 (= H413), E453 (= E484), E529 (= E548), H532 (= H551), W560 (= W579), F593 (= F614)
- binding magnesium ion: E408 (= E438), H410 (= H440), E453 (= E484)
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
34% identity, 94% coverage: 29:993/1022 of query aligns to 14:993/1022 of 5a1aA
- active site: D200 (= D227), H356 (= H380), H390 (= H413), E415 (= E438), H417 (= H440), E460 (= E484), Y502 (= Y525), E536 (= E548), N596 (≠ S610), F600 (= F614), N603 (= N617)
- binding magnesium ion: D14 (≠ E29), W15 (= W30), N17 (≠ S32), V20 (≠ A35), Q162 (= Q189), D192 (≠ S219), E415 (= E438), H417 (= H440), E460 (= E484)
- binding sodium ion: D200 (= D227), H539 (= H551), F555 (= F567), Y558 (≠ E570), P559 (= P571), L561 (≠ A573), F600 (= F614), N603 (= N617)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (= N121), D200 (= D227), M501 (= M524), Y502 (= Y525), H539 (= H551), D597 (≠ F611), F600 (= F614)
Sites not aligning to the query:
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
34% identity, 94% coverage: 29:993/1022 of query aligns to 16:995/1024 of P00722
- D202 (= D227) 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 (= H380) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H413) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E438) binding
- H419 (= H440) binding
- E462 (= E484) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E548) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H551) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ S610) binding
- F602 (= F614) mutation to A: Decreases the stability of the loop 794-804.
- G795 (≠ R796) mutation to A: It forces the apoenzyme to adopt the closed rather than the open conformation. Reduces the binding affinity.
- E798 (≠ N799) 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.
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jywA
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), Q525 (≠ E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (= N121), D189 (= D227), E449 (= E484), Y491 (= Y525), Q525 (≠ E548), H528 (= H551), N592 (= N617)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
Sites not aligning to the query:
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jyvA
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), Q525 (≠ E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (= N121), N90 (= N121), V91 (≠ E122), D189 (= D227), H406 (= H440), E449 (= E484), Y491 (= Y525), H528 (= H551), D586 (≠ F611), F589 (= F614), N592 (= N617), V783 (≠ D797), V783 (≠ D797), E785 (≠ N799), R788 (= R802)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
Sites not aligning to the query:
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 3:982/1011 of 1jynA
- active site: D189 (= D227), H345 (= H380), H379 (= H413), E404 (= E438), H406 (= H440), E449 (= E484), Y491 (= Y525), Q525 (≠ E548), N585 (≠ S610), F589 (= F614), N592 (= N617)
- binding beta-D-glucopyranose: N90 (= N121)
- binding beta-D-galactopyranose: N90 (= N121), D189 (= D227), E449 (= E484), Y491 (= Y525), H528 (= H551), N592 (= N617)
- binding magnesium ion: D3 (≠ E29), N6 (≠ S32), V9 (≠ A35), Q151 (= Q189), D181 (≠ S219), E404 (= E438), H406 (= H440), E449 (= E484)
- binding sodium ion: D189 (= D227), F544 (= F567), Y547 (≠ E570), P548 (= P571), L550 (≠ A573), F589 (= F614), N592 (= N617), S635 (≠ L663), D636 (≠ N664), E638 (≠ Y666), L658 (≠ V687), F919 (≠ T923), P920 (= P924), L955 (= L966), M956 (≠ E967), T958 (≠ A969)
Sites not aligning to the query:
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 13:992/1021 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 (= N121), D199 (= D227), E459 (= E484), Y501 (= Y525), Q535 (≠ E548), H538 (= H551), N602 (= N617)
- binding magnesium ion: D13 (≠ E29), N16 (≠ S32), V19 (≠ A35), Q161 (= Q189), D191 (≠ S219), E414 (= E438), H416 (= H440), E459 (= E484)
Sites not aligning to the query:
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 13:992/1021 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 (= N121), D199 (= D227), H389 (= H413), H416 (= H440), E459 (= E484), Y501 (= Y525), Q535 (≠ E548), H538 (= H551), W566 (= W579)
- binding magnesium ion: D13 (≠ E29), N16 (≠ S32), V19 (≠ A35), Q161 (= Q189), D191 (≠ S219), E414 (= E438), H416 (= H440), E459 (= E484)
Sites not aligning to the query:
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 15:994/1023 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 (= N121), D201 (= D227), H391 (= H413), N460 (= N483), E461 (= E484), Y503 (= Y525), F512 (vs. gap), Q537 (≠ E548), W568 (= W579)
- binding magnesium ion: D15 (≠ E29), N18 (≠ S32), V21 (≠ A35), Q163 (= Q189), D193 (≠ S219), D201 (= D227), E416 (= E438), H418 (= H440), E461 (= E484)
Sites not aligning to the query:
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
33% identity, 94% coverage: 29:993/1022 of query aligns to 7:986/1015 of 4duxA
- active site: D193 (= D227), H349 (= H380), H383 (= H413), E408 (= E438), H410 (= H440), E453 (= E484), Y495 (= Y525), E529 (= E548), N589 (≠ S610), F593 (= F614), N596 (= N617)
- binding beta-L-ribopyranose: D193 (= D227), H383 (= H413), E453 (= E484), M494 (= M524), Y495 (= Y525), E529 (= E548), H532 (= H551), W560 (= W579), F593 (= F614), S788 (≠ R798)
- binding magnesium ion: D7 (≠ E29), N10 (≠ S32), V13 (≠ A35), Q155 (= Q189), D185 (≠ S219), E408 (= E438), H410 (= H440), E453 (= E484)
Sites not aligning to the query:
6secA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cbon complex with onpg (see paper)
32% identity, 93% coverage: 69:1018/1022 of query aligns to 37:985/988 of 6secA
6sebA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cb in complex with iptg (see paper)
32% identity, 93% coverage: 69:1018/1022 of query aligns to 37:985/989 of 6sebA
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: D186 (= D227), E420 (= E484), Y461 (= Y525), E496 (= E548), H499 (= H551), D887 (≠ F918), R939 (≠ I972), L942 (= L975), K943 (≠ E976), A944 (≠ R977), C964 (= C997)
Query Sequence
>351154 FitnessBrowser__Btheta:351154
MKLKKRTFLILMAALTATFASAQKQPLPEWQSQYAVGLNKLAPHTYVWPYADASDIGKPG
GYEQSPYYMSLNGKWKFNWVKNPDNRPKDFYQPSYYTGGWADINVPGNWERQGYGTAIYV
NETYEFDDKMFNFKKNPPLVPFAENEVGSYRRTFKVPADWKGRRVVLCCEGVISFYYVWV
NGKLLGYNQGSKTAAEWDITDVLSEGENVVALEVYRWSSGAYLECQDMWRLSGIERDVYL
YSTPKQYIADYKVSASLDKEKYKEGIFNLEVTVEGPSATASSIAYTLKDASGKAVLQDAI
NIKSRGLSNFIAFDEKKIAEVKAWNAEHPNLYTLVLELKDAQGKVTELTGCEVGFRTSEI
KDGRFCINGVPVLVKGTNRHEHSQLGRTVSKELMEQDIRLMKQHNINMVRNSHYPTHPYW
YQLCDRYGLYMIDEANIESHGMGYGPASLAKDSTWLTAHMDRTHRMYERSKNHPAIVIWS
QGNEAGNGINFERTYDWLKSVEKGRPVQYERAELNYNTDIYCRMYRSVDEIKAYVGKKDI
YRPFILCEYLHAMGNSCGGMKEYWEVFENEPMAQGGCIWDWVDQNFREIDKDGKWYWTYG
GDYGPEGIPSFGNFCGNGLVNAVREPHPHLLEVKKIYQNIKATLSDRKNLKVCIKNWYDF
SNLNEYILRWNVKGEDGTVLAEGTKEVDCEPHATVDVTLGAVKLPNTVREAYLNLSWSRK
EATPLVDTDWEVAYDQFVLAGNKNTTAYRPQKAGETAFVVDKNTGALSSLTLDGKELLAA
PITLSLFRPATDNDNRDRNGARLWRKAGLNNLTQKVVSLKEEKTSATVRAEILNGKGQKV
GMADFVYALDKNGALKVRTTFQPDTAIVKSMARLGLTFRMADAYNQVSYLGRGDHETYID
RNQSGRIGLYDTTVERMFHYYATPQSTANRTDVRWAKLTDQAGEGVFMESNRPFQFSIIP
FSDVLLEKAHHINELERDGMITIHLDAEQAGVGTATCGPGVLPQYLVPVKKQSFEFTLYP
VK
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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