SitesBLAST
Comparing 5210843 FitnessBrowser__PV4:5210843 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)
40% identity, 97% coverage: 35:1074/1076 of query aligns to 4:992/1083 of 6s6zA
3bgaA Crystal structure of beta-galactosidase from bacteroides thetaiotaomicron vpi-5482
37% identity, 96% coverage: 35:1064/1076 of query aligns to 4:995/1003 of 3bgaA
- active site: D201 (= D224), H354 (= H376), H387 (= H410), E412 (= E435), H414 (= H437), E458 (= E482), Y499 (= Y523), E522 (= E545), S584 (≠ T606), F588 (= F610), N591 (= N613)
- binding magnesium ion: E412 (= E435), H414 (= H437), E458 (= E482)
P00722 Beta-galactosidase; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see 13 papers)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 11:1012/1024 of P00722
- D202 (= D224) 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 (= H376) mutation H->D,F,L,N: Less stable to heat than wild-type. Causes significant destabilizations of the first transition state.
- H392 (= H410) mutation H->E,F,K: Essentially inactive unless very rapid purification. Causes very large destabilizations of the transition state.
- E417 (= E435) binding
- H419 (= H437) binding
- E462 (= E482) active site, Proton donor; binding ; mutation to H: Slowly inactivates galactosidase activity by reducing the binding of magnesium. It increases binding specificity.
- E538 (= E545) active site, Nucleophile; mutation to Q: 10000-fold decrease in the beta-galactosidase activity.
- H541 (= H548) mutation H->E,F,N: Poorly reactive with galactosyl substrates. Less stable to heat than wild-type.
- N598 (≠ T606) binding
- F602 (= F610) mutation to A: Decreases the stability of the loop 794-804.
- G795 (= G811) 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.
- W1000 (= W1040) mutation W->F,G,L,T: Decreases affinity for substrate.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5a1aA 2.2 a resolution cryo-em structure of beta-galactosidase in complex with a cell-permeant inhibitor (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 9:1010/1022 of 5a1aA
- active site: D200 (= D224), H356 (= H376), H390 (= H410), E415 (= E435), H417 (= H437), E460 (= E482), Y502 (= Y523), E536 (= E545), N596 (≠ T606), F600 (= F610), N603 (= N613)
- binding magnesium ion: D14 (≠ R34), W15 (= W35), N17 (≠ D37), V20 (≠ L40), Q162 (= Q186), D192 (= D216), E415 (= E435), H417 (= H437), E460 (= E482)
- binding sodium ion: D200 (= D224), H539 (= H548), F555 (≠ I564), Y558 (= Y567), P559 (= P568), L561 (= L570), F600 (= F610), N603 (= N613)
- binding 2-phenylethyl 1-thio-beta-D-galactopyranoside: N101 (≠ D125), D200 (= D224), M501 (= M522), Y502 (= Y523), H539 (= H548), D597 (= D607), F600 (= F610), W998 (= W1040)
6tshA Beta-galactosidase in complex with deoxygalacto-nojirimycin (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 2:1003/1015 of 6tshA
- binding (2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol: D193 (= D224), H383 (= H410), E453 (= E482), E529 (= E545), H532 (= H548), W560 (= W576), F593 (= F610)
- binding magnesium ion: E408 (= E435), H410 (= H437), E453 (= E482)
1jz6A E. Coli (lacz) beta-galactosidase in complex with galacto-tetrazole (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jz6A
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), E525 (= E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding (5r, 6s, 7s, 8s)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-a]piperidine: D189 (= D224), H379 (= H410), E449 (= E482), Y491 (= Y523), E525 (= E545), H528 (= H548), W556 (= W576), N592 (= N613)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482), S635 (≠ T661), E638 (≠ L664), L658 (≠ M684)
- binding sodium ion: D189 (= D224), F544 (≠ I564), Y547 (= Y567), P548 (= P568), L550 (= L570), F589 (= F610), C590 (≠ L611), N592 (= N613), F919 (≠ R934), P920 (= P935), L955 (= L1006), M956 (≠ V1007), T958 (≠ V1009)
1jz5A E. Coli (lacz) beta-galactosidase in complex with d-galctopyranosyl-1- on (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jz5A
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), E525 (= E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding D-galactonolactone: D189 (= D224), H379 (= H410), N448 (= N481), E449 (= E482), M490 (= M522), Y491 (= Y523), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F610), N592 (= N613)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
1jz3A E. Coli (lacz) beta-galactosidase-trapped 2-deoxy-galactosyl enzyme intermediate (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jz3A
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), E525 (= E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding 2-deoxy-alpha-D-galactopyranose: D189 (= D224), H379 (= H410), E449 (= E482), Y491 (= Y523), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F610)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
1jz2A E. Coli (lacz) beta-galactosidase-trapped 2-f-galactosyl-enzyme intermediate (orthorhombic) (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jz2A
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), E525 (= E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding 2-deoxy-2-fluoro-beta-D-galactopyranose: D189 (= D224), H379 (= H410), N448 (= N481), E449 (= E482), Y491 (= Y523), E525 (= E545), H528 (= H548), W556 (= W576), F589 (= F610)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
- binding sodium ion: D189 (= D224), F544 (≠ I564), Y547 (= Y567), P548 (= P568), L550 (= L570), Q551 (= Q571), F589 (= F610), N592 (= N613), F919 (≠ R934), P920 (= P935), L955 (= L1006), M956 (≠ V1007), T958 (≠ V1009)
1jyxA E. Coli (lacz) beta-galactosidase in complex with iptg (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jyxA
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), E525 (= E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding 1-methylethyl 1-thio-beta-D-galactopyranoside: N90 (≠ D125), D189 (= D224), E292 (= E323), P294 (= P325), E449 (= E482), E525 (= E545), H528 (= H548), N592 (= N613), R633 (≠ A659), D636 (≠ S662), Q690 (≠ T721), W696 (≠ P727), W987 (= W1040)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
- binding sodium ion: D189 (= D224), F544 (≠ I564), Y547 (= Y567), P548 (= P568), L550 (= L570), Q551 (= Q571), F589 (= F610), C590 (≠ L611), N592 (= N613), F919 (≠ R934), P920 (= P935), L955 (= L1006), M956 (≠ V1007), T958 (≠ V1009)
7btkC E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa01 (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 10:1011/1023 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 (≠ D125), D201 (= D224), H391 (= H410), N460 (= N481), E461 (= E482), Y503 (= Y523), F512 (vs. gap), Q537 (≠ E545), W568 (= W576), W999 (= W1040)
- binding magnesium ion: D15 (≠ R34), N18 (≠ D37), V21 (≠ L40), Q163 (= Q186), D193 (= D216), D201 (= D224), E416 (= E435), H418 (= H437), E461 (= E482)
7brsA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksa02 (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 8:1009/1021 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 (≠ D125), D199 (= D224), E459 (= E482), Y501 (= Y523), Q535 (≠ E545), H538 (= H548), N602 (= N613), W997 (= W1040)
- binding magnesium ion: D13 (≠ R34), N16 (≠ D37), V19 (≠ L40), Q161 (= Q186), D191 (= D216), E414 (= E435), H416 (= H437), E459 (= E482)
6kuzA E.Coli beta-galactosidase (e537q) in complex with fluorescent probe ksl01 (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 8:1009/1021 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 (≠ D125), D199 (= D224), H389 (= H410), H416 (= H437), E459 (= E482), Y501 (= Y523), Q535 (≠ E545), H538 (= H548), W566 (= W576), W997 (= W1040)
- binding magnesium ion: D13 (≠ R34), N16 (≠ D37), V19 (≠ L40), Q161 (= Q186), D191 (= D216), E414 (= E435), H416 (= H437), E459 (= E482)
4duxA E. Coli (lacz) beta-galactosidase (n460s) in complex with l-ribose (see paper)
34% identity, 95% coverage: 29:1052/1076 of query aligns to 2:1003/1015 of 4duxA
- active site: D193 (= D224), H349 (= H376), H383 (= H410), E408 (= E435), H410 (= H437), E453 (= E482), Y495 (= Y523), E529 (= E545), N589 (≠ T606), F593 (= F610), N596 (= N613)
- binding beta-L-ribopyranose: D193 (= D224), H383 (= H410), E453 (= E482), M494 (= M522), Y495 (= Y523), E529 (= E545), H532 (= H548), W560 (= W576), F593 (= F610), S788 (≠ Q813), W991 (= W1040)
- binding magnesium ion: D7 (≠ R34), N10 (≠ D37), V13 (≠ L40), Q155 (= Q186), D185 (= D216), E408 (= E435), H410 (= H437), E453 (= E482)
1jywA E. Coli (lacz) beta-galactosidase (e537q) in complex with pnpg (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jywA
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), Q525 (≠ E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding 4-nitrophenyl beta-D-galactopyranoside: N90 (≠ D125), D189 (= D224), E449 (= E482), Y491 (= Y523), Q525 (≠ E545), H528 (= H548), N592 (= N613), W987 (= W1040)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
1jyvA E. Coli (lacz) beta-galactosidase (e537q) in complex with onpg (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jyvA
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), Q525 (≠ E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding 2-nitrophenyl beta-D-galactopyranoside: N90 (≠ D125), N90 (≠ D125), V91 (≠ E126), D189 (= D224), H406 (= H437), E449 (= E482), Y491 (= Y523), H528 (= H548), D586 (= D607), F589 (= F610), N592 (= N613), V783 (≠ N812), V783 (≠ N812), E785 (vs. gap), R788 (vs. gap), W987 (= W1040)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
1jynA E. Coli (lacz) beta-galactosidase (e537q) in complex with lactose (see paper)
34% identity, 95% coverage: 32:1052/1076 of query aligns to 1:999/1011 of 1jynA
- active site: D189 (= D224), H345 (= H376), H379 (= H410), E404 (= E435), H406 (= H437), E449 (= E482), Y491 (= Y523), Q525 (≠ E545), N585 (≠ T606), F589 (= F610), N592 (= N613)
- binding beta-D-glucopyranose: N90 (≠ D125), W987 (= W1040)
- binding beta-D-galactopyranose: N90 (≠ D125), D189 (= D224), E449 (= E482), Y491 (= Y523), H528 (= H548), N592 (= N613), W987 (= W1040)
- binding magnesium ion: D3 (≠ R34), N6 (≠ D37), V9 (≠ L40), Q151 (= Q186), D181 (= D216), E404 (= E435), H406 (= H437), E449 (= E482)
- binding sodium ion: D189 (= D224), F544 (≠ I564), Y547 (= Y567), P548 (= P568), L550 (= L570), F589 (= F610), N592 (= N613), S635 (≠ T661), D636 (≠ S662), E638 (≠ L664), L658 (≠ M684), F919 (≠ R934), P920 (= P935), L955 (= L1006), M956 (≠ V1007), T958 (≠ V1009)
P06864 Evolved beta-galactosidase subunit alpha; Beta-gal; Lactase; EC 3.2.1.23 from Escherichia coli (strain K12) (see paper)
31% identity, 96% coverage: 33:1065/1076 of query aligns to 2:1001/1030 of P06864
- E449 (= E482) active site, Proton donor
6sebA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cb in complex with iptg (see paper)
33% identity, 82% coverage: 73:949/1076 of query aligns to 37:907/989 of 6sebA
Sites not aligning to the query:
6secA Cold-adapted beta-d-galactosidase from arthrobacter sp. 32cbon complex with onpg (see paper)
33% identity, 82% coverage: 73:949/1076 of query aligns to 37:907/988 of 6secA
Query Sequence
>5210843 FitnessBrowser__PV4:5210843
MINRFSLLQRLSYTLAFSLVFGLVVSNPALARDRWQDHTLFEVNKLAPHASFFGYESEPL
ALLDEMDRSQLYLDLNGRWRFHLAKNPDATPKEFAAPEFDASHWGSIQVPGNFETQGYGH
AIYLDERYPFDTKWPDAPSDHNPTGLYRKTFTLPAHWQQKQVFIHIGAARSALTLFVNGR
EVGYSQGAKTPAEFDITPYLQAGDNLVAMQLIRWSDASYLESQDMLRMTGIEREVYLYAT
PKQRIEDIQVVTHLNEDLTRAKLAIRVDIASHQPGVRALELEARLLDPQGKPVAKANQRL
SLKGDAKPVFSQTLISPKLWNAEMPNLYRLILTLKTEKGETLQVASQQIGVRKIAIENGQ
LKVNNKAITIRGVDRHETDPQTGHVVSRETMELDIRLMKQNNINAVRSSHYPNHPYWLSL
ADRYGLYVIDEANIESHPLAIDDKTQLGNEMSWLPAHQARIERMVERDKNHPSVIIWSLG
NEAGEGKLFERLYQWIKRRDPNRPVQYEPAGEAPYTDIVAPMYPSIERIREYAERASDRP
LIMIEYAHAMGNSVGNLQDYWDVIEAYPQLQGGFIWDWVDQALAFSNDLGQRYWAYGKDY
HPDMPTDGNFLNNGLVDPDRNPHPHLSEVKKVYQPIKLRDFKVEGDKASVNLINGFDFAS
TSGLSLNWTLQKDGKIIASKRQAMPILSPGEQARVSLTLPGKQSLSAPFEYHLLLEVLVD
TPRPLLPSDLRIAFEQFALPRFGTKAAYQVKKNQAKISEDSGSYRLTSGELSYEFDKRSG
WLTQIYQEGEPQLKAPLMANFWRAPTDNDLGNQMPDWAGAWQDAATELEVTAIDADLALG
LTISQTHAEKGFSLRTRYSLDNAGRLMVDSQFIPGNKPLADLPRFGFSTRLGFEHRYLSY
FGRGPEETYADRQSGNPLGWYALPIEQTYHRYPRPQETGQRTQVRYAAVTDQRGQGWLAI
ANQAHAGEQDRKEADEVATLQTSLWPFAQADIDFRRGDAQDSASGLVAVTRNHGAEIPLR
EFVTWNIDYRQMGVGGDTSWGRPVHGPYRIKAEPIRFGFTLMPVSSDDDIRTLARQ
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