SitesBLAST
Comparing GFF3062 FitnessBrowser__psRCH2:GFF3062 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)
P0AC81 Lactoylglutathione lyase; Aldoketomutase; Glyoxalase I; Glx I; Ketone-aldehyde mutase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase; EC 4.4.1.5 from Escherichia coli (strain K12) (see paper)
64% identity, 99% coverage: 1:129/130 of query aligns to 1:129/135 of P0AC81
- H5 (= H5) binding
- E56 (= E56) binding
- H74 (= H74) binding in other chain
- E122 (= E122) binding in other chain
1fa6A Crystal structure of the co(ii)-bound glyoxalase i of escherichia coli (see paper)
65% identity, 95% coverage: 1:124/130 of query aligns to 1:124/128 of 1fa6A
1fa5A Crystal structure of the zn(ii)-bound glyoxalase i of escherichia coli (see paper)
65% identity, 95% coverage: 1:124/130 of query aligns to 1:124/128 of 1fa5A
4mttA Ni- and zn-bound gloa2 at low resolution (see paper)
58% identity, 96% coverage: 1:125/130 of query aligns to 1:125/128 of 4mttA
6bnnA Crystal structure of v278e-glyoxalase i mutant from zea mays in space group p4(1)2(1)2 (see paper)
54% identity, 99% coverage: 2:130/130 of query aligns to 16:142/282 of 6bnnA
Sites not aligning to the query:
5d7zA Crystal structure of glyoxalase i from zea mays (see paper)
54% identity, 99% coverage: 2:130/130 of query aligns to 10:136/281 of 5d7zA
Sites not aligning to the query:
Q948T6 Lactoylglutathione lyase; Aldoketomutase; Allergen Glb33; Glyoxalase I; Glx I; Glyoxylase I 11; OsGLYI-11; OsGLYI11; Ketone-aldehyde mutase; Methylglyoxalase; PP33; S-D-lactoylglutathione methylglyoxal lyase; Allergen Ory s Glyoxalase I; EC 4.4.1.5 from Oryza sativa subsp. japonica (Rice) (see paper)
53% identity, 95% coverage: 2:125/130 of query aligns to 24:148/291 of Q948T6
- E78 (= E56) mutation to Q: No effect on the activity.
- E145 (= E122) mutation to Q: Loss of activity.
Sites not aligning to the query:
- 209 E→D: Loss of activity.
2c21A Specificity of the trypanothione-dependednt leishmania major glyoxalase i: structure and biochemical comparison with the human enzyme (see paper)
52% identity, 97% coverage: 2:127/130 of query aligns to 3:123/139 of 2c21A
Q9CPU0 Lactoylglutathione lyase; Aldoketomutase; Glyoxalase I; Glx I; Ketone-aldehyde mutase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase; EC 4.4.1.5 from Mus musculus (Mouse) (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 32:179/184 of Q9CPU0
- Q34 (≠ H5) binding
- E100 (= E56) binding
- H127 (= H74) binding in other chain
- E173 (= E122) binding in other chain
3w0uA Human glyoxalase i with an n-hydroxypyridone inhibitor
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/175 of 3w0uA
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding N-[3-(1-Hydroxy-6-oxo-4-phenyl-1,6-dihydro-pyridin-2-yl)-5-methanesulfonylamino-phenyl]-methanesulfonamide: Q26 (≠ H5), F60 (= F39), L62 (= L41), E92 (= E56), H119 (= H74), K143 (≠ R98), M150 (= M104), E165 (= E122)
- binding zinc ion: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
Sites not aligning to the query:
Q04760 Lactoylglutathione lyase; Aldoketomutase; Glyoxalase I; Glx I; Ketone-aldehyde mutase; Methylglyoxalase; S-D-lactoylglutathione methylglyoxal lyase; EC 4.4.1.5 from Homo sapiens (Human) (see 12 papers)
42% identity, 97% coverage: 3:128/130 of query aligns to 32:179/184 of Q04760
- Q34 (≠ H5) binding ; mutation to E: Reduces enzyme activity by 99%.
- S45 (= S16) mutation to A: No effect on phosphorylation.
- C61 (≠ K32) modified: Disulfide link with 139, Alternate; mutation to A: No effect on NO-mediated modification.
- S69 (≠ T40) mutation to A: No effect on phosphorylation.
- S94 (≠ A50) mutation to A: No effect on phosphorylation.
- T98 (≠ V54) mutation to A: No effect on phosphorylation.
- E100 (= E56) binding ; mutation to Q: Reduces enzyme activity by over 99%.
- T102 (= T58) mutation to A: No effect on phosphorylation.
- T107 (≠ V63) modified: Phosphothreonine; mutation to A: Loss of phosphorylation.
- E111 (vs. gap) to A: in dbSNP:rs4746
- H127 (= H74) binding in other chain
- C139 (= C86) modified: S-glutathionyl cysteine; alternate; modified: Disulfide link with 61, Alternate; mutation to A: Impaired NO-mediated modification. Loss of NO-mediated modification; when associated with A-19 or A-20.
- E173 (= E122) active site, Proton donor/acceptor; binding in other chain; mutation to Q: Abolishes enzyme activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 19 modified: Disulfide link with 20; C → Y: in dbSNP:rs17855424; C→A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-20. Loss of NO-mediated modification; when associated with A-139.
- 20 modified: Disulfide link with 19; C→A: No effect on NO-mediated modification. Impaired NO-mediated modification; when associated with A-19. Loss of NO-mediated modification; when associated with A-139.
3w0tA Human glyoxalase i with an n-hydroxypyridone derivative inhibitor
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/176 of 3w0tA
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding N-[3-(1-hydroxy-6-oxo-4-phenyl-1,6-dihydropyridin-2-yl)phenyl]methanesulfonamide: Q26 (≠ H5), F55 (≠ Y34), F60 (= F39), L62 (= L41), F64 (= F43), E92 (= E56), H119 (= H74), E165 (= E122)
- binding zinc ion: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
Sites not aligning to the query:
3vw9A Human glyoxalase i with an n-hydroxypyridone inhibitor (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/176 of 3vw9A
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding 1-hydroxy-6-[1-(3-methoxypropyl)-1H-pyrrolo[2,3-b]pyridin-5-yl]-4-phenylpyridin-2(1H)-one: Q26 (≠ H5), C53 (≠ K32), L62 (= L41), E92 (= E56), H119 (= H74), M150 (= M104), F155 (= F112), E165 (= E122)
- binding zinc ion: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
Sites not aligning to the query:
1qipA Human glyoxalase i complexed with s-p- nitrobenzyloxycarbonylglutathione (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/176 of 1qipA
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding s-p-nitrobenzyloxycarbonylglutathione: R30 (= R9), Q51 (≠ R30), C53 (≠ K32), F60 (= F39), F64 (= F43), I81 (vs. gap), L85 (vs. gap), T94 (= T58), N96 (= N60), R115 (vs. gap), M150 (= M104), F155 (= F112)
- binding zinc ion: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
Sites not aligning to the query:
1qinA Human glyoxalase i complexed with s-(n-hydroxy-n-p- iodophenylcarbamoyl) glutathione (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/176 of 1qinA
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding s-(n-hydroxy-n-iodophenylcarbamoyl)glutathione: Q26 (≠ H5), R30 (= R9), F60 (= F39), L62 (= L41), F64 (= F43), E92 (= E56), T94 (= T58), N96 (= N60), R115 (vs. gap), H119 (= H74), K143 (≠ R98), G148 (vs. gap), K149 (≠ M103), M150 (= M104), E165 (= E122)
- binding zinc ion: Q26 (≠ H5), E92 (= E56)
Sites not aligning to the query:
1froA Human glyoxalase i with benzyl-glutathione inhibitor (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 24:171/176 of 1froA
- active site: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
- binding s-benzyl-glutathione: R30 (= R9), F60 (= F39), T94 (= T58), N96 (= N60), R115 (vs. gap), M150 (= M104), F155 (= F112), E165 (= E122)
- binding zinc ion: Q26 (≠ H5), E92 (= E56), H119 (= H74), E165 (= E122)
Sites not aligning to the query:
7wt0A Human glyoxalase i (with c-ter his tag) in complex with tlsc702 (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 31:178/185 of 7wt0A
- binding (~{E})-3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid: C60 (≠ K32), F62 (≠ Y34), L69 (= L41), F71 (= F43), L92 (vs. gap), E99 (= E56), H126 (= H74), K150 (≠ R98), M157 (= M104), L160 (= L110), F162 (= F112), E172 (= E122)
- binding zinc ion: Q33 (≠ H5), E99 (= E56), H126 (= H74), E172 (= E122)
Sites not aligning to the query:
4x2aA Crystal structure of mouse glyoxalase i complexed with baicalein (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 18:165/167 of 4x2aA
- active site: Q20 (≠ H5), E86 (= E56), H113 (= H74), E159 (= E122)
- binding 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one: Q20 (≠ H5), F49 (≠ Y34), L56 (= L41), F79 (vs. gap), E86 (= E56), H113 (= H74), M144 (= M104), E159 (= E122)
- binding zinc ion: Q20 (≠ H5), E86 (= E56), H113 (= H74), E159 (= E122)
Sites not aligning to the query:
4kyhA Crystal structure of mouse glyoxalase i complexed with zopolrestat (see paper)
42% identity, 97% coverage: 3:128/130 of query aligns to 27:174/177 of 4kyhA
- active site: Q29 (≠ H5), E95 (= E56), H122 (= H74), E168 (= E122)
- binding zinc ion: Q29 (≠ H5), E95 (= E56), H122 (= H74), E168 (= E122)
- binding 3,4-dihydro-4-oxo-3-((5-trifluoromethyl-2-benzothiazolyl)methyl)-1-phthalazine acetic acid: M31 (= M7), R33 (= R9), F63 (= F39), E95 (= E56), T97 (= T58), N99 (= N60)
6l0uB Crystal structure of mouse glyoxalase i complexed with a small molecule inhibitor
42% identity, 97% coverage: 3:128/130 of query aligns to 25:172/177 of 6l0uB
- active site: Q27 (≠ H5), E93 (= E56), H120 (= H74), E166 (= E122)
- binding N-[4-(trifluoromethyloxy)phenyl]-1,3,4,9-tetrahydropyrido[3,4-b]indole-2-carbothioamide: R116 (vs. gap), K144 (≠ R98), D148 (≠ P102), G149 (vs. gap), W164 (≠ K120)
- binding zinc ion: Q27 (≠ H5), E93 (= E56), H120 (= H74), E166 (= E122)
Query Sequence
>GFF3062 FitnessBrowser__psRCH2:GFF3062
MRLLHTMLRVGDMDKSIAFYTEVLGMTLLRRKDYPDGKFTLAFVGYGDEAHNSVIELTHN
WGVETYELGNGYGHIALEVEDVYKACEDIRARGGKITREPGPMMHGSSILAFVEDPDGYK
IELLSPKRAD
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