SitesBLAST
Comparing 350360 FitnessBrowser__Btheta:350360 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)
O53289 Phosphoserine phosphatase SerB2; PSP; PSPase; O-phosphoserine phosphohydrolase; Protein-serine/threonine phosphatase; EC 3.1.3.3; EC 3.1.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
38% identity, 96% coverage: 9:401/409 of query aligns to 7:385/409 of O53289
- G18 (= G20) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- G108 (≠ R113) mutation to A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- D185 (= D201) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M202) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D203) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S204) mutation to A: No effect on enzymatic activity.
- S273 (= S289) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K334) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D357) mutation to G: Decreases enzymatic activity by 80%.; mutation to N: Decreases enzymatic activity by 85%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-345.
- D345 (= D361) mutation to N: Decreases enzymatic activity by 55%. Completely abolishes enzymatic activity, does not elicit cytoskeletal rearrangements, and does not suppress IL-8 production after TNF-alpha stimulation; when associated with N-341.
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
37% identity, 96% coverage: 9:401/409 of query aligns to 5:383/396 of 8a21A
- binding magnesium ion: D183 (= D201), D185 (= D203), D339 (= D357)
- binding 4-phenyl-1h-imidazole: D13 (= D17), T18 (= T22), Q37 (= Q41), D185 (= D203), E192 (= E210), V193 (= V211), I194 (= I212), T211 (= T229), M215 (= M233), F221 (= F239), R228 (= R246), G273 (= G291)
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
37% identity, 96% coverage: 9:401/409 of query aligns to 5:383/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D203), E192 (= E210), M215 (= M233), F221 (= F239), L225 (≠ F243), R228 (= R246), G272 (= G290), F274 (= F292), D339 (= D357)
- binding magnesium ion: D183 (= D201), D185 (= D203), D339 (= D357)
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
37% identity, 96% coverage: 9:401/409 of query aligns to 5:383/396 of 5jlpA
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
37% identity, 96% coverage: 9:402/409 of query aligns to 9:388/411 of A0QJI1
- D187 (= D201) binding
- D189 (= D203) binding
- D343 (= D357) binding
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
44% identity, 51% coverage: 193:400/409 of query aligns to 2:209/210 of 1f5sA
- active site: D10 (= D201), F11 (≠ M202), D12 (= D203), G99 (= G290), K143 (= K334), D170 (= D361)
- binding magnesium ion: D10 (= D201), D12 (= D203), D166 (= D357)
- binding phosphate ion: D10 (= D201), F11 (≠ M202), D12 (= D203), S98 (= S289), G99 (= G290), K143 (= K334)
Q58989 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see 3 papers)
44% identity, 51% coverage: 193:400/409 of query aligns to 3:210/211 of Q58989
- D11 (= D201) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D203) active site, Proton donor; binding
- E20 (= E210) binding
- R56 (= R246) binding
- SG 99:100 (= SG 289:290) binding
- K144 (= K334) binding
- D167 (= D357) binding
- N170 (= N360) binding
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
44% identity, 51% coverage: 193:400/409 of query aligns to 1:208/209 of 1l7nA
- active site: D9 (= D201), F10 (≠ M202), D11 (= D203), G98 (= G290), K142 (= K334), D169 (= D361)
- binding aluminum fluoride: D9 (= D201), F10 (≠ M202), D11 (= D203), S97 (= S289), K142 (= K334)
- binding tetrafluoroaluminate ion: D9 (= D201), F10 (≠ M202), D11 (= D203), S97 (= S289), G98 (= G290), K142 (= K334), N168 (= N360)
- binding magnesium ion: D9 (= D201), D11 (= D203), D165 (= D357)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
44% identity, 50% coverage: 195:400/409 of query aligns to 2:207/208 of 1l7pA
- active site: N8 (≠ D201), F9 (≠ M202), D10 (= D203), G97 (= G290), K141 (= K334), D168 (= D361)
- binding phosphoserine: N8 (≠ D201), F9 (≠ M202), D10 (= D203), E17 (= E210), M40 (= M233), F46 (= F239), R53 (= R246), S96 (= S289), G97 (= G290), K141 (= K334)
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
43% identity, 52% coverage: 192:405/409 of query aligns to 77:291/295 of 7qplA
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
43% identity, 50% coverage: 195:400/409 of query aligns to 2:199/200 of 1l7oA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 48% coverage: 194:389/409 of query aligns to 2:196/208 of 3m1yC
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
33% identity, 47% coverage: 198:388/409 of query aligns to 13:209/217 of 6q6jB
- binding calcium ion: D16 (= D201), D18 (= D203), D175 (= D357)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D201), V17 (≠ M202), D18 (= D203), F54 (= F239), S105 (= S289), G106 (= G290), G107 (= G291), K154 (= K334), T178 (≠ N360)
6hyjB Psph human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 198:388/409 of query aligns to 17:213/223 of 6hyjB
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
33% identity, 47% coverage: 198:388/409 of query aligns to 13:209/221 of 6hyyA
P78330 Phosphoserine phosphatase; PSP; PSPase; L-3-phosphoserine phosphatase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Homo sapiens (Human) (see 4 papers)
33% identity, 47% coverage: 198:388/409 of query aligns to 17:213/225 of P78330
- D20 (= D201) binding
- DVD 20:22 (≠ DMD 201:203) binding
- D22 (= D203) binding
- S23 (= S204) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E210) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D213) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A216) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M233) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ R234) binding
- R65 (= R246) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 289:291) binding ; binding
- N133 (= N311) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K334) binding ; binding
- D179 (= D357) binding
- T182 (≠ N360) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
- R202 (≠ K377) mutation to A: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to K: Reduces L-phosphoserine phosphatase activity by about 95%.
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 198:388/409 of query aligns to 14:210/222 of 1l8oA
- active site: D17 (= D201), V18 (≠ M202), D19 (= D203), G107 (= G290), K155 (= K334), D180 (= D361)
- binding phosphate ion: D17 (= D201), D19 (= D203), S106 (= S289), K155 (= K334)
- binding serine: G177 (= G358), T179 (≠ N360), R199 (≠ K377)
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 47% coverage: 198:388/409 of query aligns to 14:210/222 of 1l8lA
- active site: D17 (= D201), V18 (≠ M202), D19 (= D203), G107 (= G290), K155 (= K334), D180 (= D361)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D201), D19 (= D203), G107 (= G290), K155 (= K334), D176 (= D357), G177 (= G358), T179 (≠ N360)
6iuyA Structure of dsgpdh of dunaliella salina (see paper)
33% identity, 28% coverage: 177:292/409 of query aligns to 4:114/585 of 6iuyA
Sites not aligning to the query:
- binding magnesium ion: 175
- binding nicotinamide-adenine-dinucleotide: 233, 234, 235, 236, 268, 290, 321, 324, 349, 381, 382, 497, 529, 530, 532
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
28% identity, 44% coverage: 194:373/409 of query aligns to 8:174/200 of 4ap9A
- active site: D15 (= D201), I16 (≠ M202), E17 (≠ D203), G103 (= G290), K141 (= K334), D162 (= D361)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ I217), I32 (≠ R218), T33 (≠ A219), L46 (≠ M233), W52 (≠ F239), D140 (≠ R333), K141 (= K334), Y160 (≠ A359), A161 (≠ N360)
Query Sequence
>350360 FitnessBrowser__Btheta:350360
MQPSNTELILIRVTGEDRPGLTASVTEILAKYDATILDIGQADIHNTLSLGILFRSEERH
SGFIMKELLFKASSLGVTIRFEPIGTDQYENWVGMQGKNRYILTVLGRKLSARQISAATR
VLAEQDLNIDAIKRLTGRIPLDEDKTDTRTRACIEFSVRGTPKDRIAMQERLMQLASEQE
MDFSFQQDNMYRRMRRLICFDMDSTLIETEVIDELAIRAGVGDEVKAITESAMRGEIDFT
ESFTRRVALLKGLDESVMQEIAESLPITEGVDRLMYVLKKYGYKIAILSGGFTYFGQYLQ
KKYGIDYVYANELEIVDGKLTGRYLGDVVDGKRKAELLRLIAQVEKVDIAQTIAVGDGAN
DLPMLGIAGLGIAFHAKPKVVANAKQSINTIGLDGVLYFLGFKDSYLNM
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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