SitesBLAST
Comparing 6936796 FitnessBrowser__SB2B:6936796 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)
1l7nA Transition state analogue of phosphoserine phosphatase (aluminum fluoride complex) (see paper)
42% identity, 66% coverage: 107:313/316 of query aligns to 1:208/209 of 1l7nA
- active site: D9 (= D115), F10 (≠ M116), D11 (= D117), G98 (= G204), K142 (= K248), D169 (= D275)
- binding aluminum fluoride: D9 (= D115), F10 (≠ M116), D11 (= D117), S97 (= S203), K142 (= K248)
- binding tetrafluoroaluminate ion: D9 (= D115), F10 (≠ M116), D11 (= D117), S97 (= S203), G98 (= G204), K142 (= K248), N168 (= N274)
- binding magnesium ion: D9 (= D115), D11 (= D117), D165 (= D271)
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)
42% identity, 66% coverage: 107:313/316 of query aligns to 3:210/211 of Q58989
- D11 (= D115) active site, Nucleophile; binding ; mutation to N: Loss of activity.
- D13 (= D117) active site, Proton donor; binding
- E20 (= E124) binding
- R56 (= R160) binding
- SG 99:100 (= SG 203:204) binding
- K144 (= K248) binding
- D167 (= D271) binding
- N170 (= N274) binding
1f5sA Crystal structure of phosphoserine phosphatase from methanococcus jannaschii (see paper)
42% identity, 66% coverage: 107:313/316 of query aligns to 2:209/210 of 1f5sA
- active site: D10 (= D115), F11 (≠ M116), D12 (= D117), G99 (= G204), K143 (= K248), D170 (= D275)
- binding magnesium ion: D10 (= D115), D12 (= D117), D166 (= D271)
- binding phosphate ion: D10 (= D115), F11 (≠ M116), D12 (= D117), S98 (= S203), G99 (= G204), K143 (= K248)
1l7pA Substrate bound phosphoserine phosphatase complex structure (see paper)
42% identity, 64% coverage: 111:313/316 of query aligns to 4:207/208 of 1l7pA
- active site: N8 (≠ D115), F9 (≠ M116), D10 (= D117), G97 (= G204), K141 (= K248), D168 (= D275)
- binding phosphoserine: N8 (≠ D115), F9 (≠ M116), D10 (= D117), E17 (= E124), M40 (= M147), F46 (= F153), R53 (= R160), S96 (= S203), G97 (= G204), K141 (= K248)
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)
45% identity, 66% coverage: 107:314/316 of query aligns to 177:384/409 of O53289
- D185 (= D115) mutation to G: Completely abolishes enzymatic activity.; mutation to N: Completely abolishes enzymatic activity.
- V186 (≠ M116) mutation to Q: Decreases enzymatic activity by 50%.
- D187 (= D117) mutation to N: Decreases enzymatic activity by 15%.
- S188 (= S118) mutation to A: No effect on enzymatic activity.
- S273 (= S203) mutation to A: Completely abolishes enzymatic activity (PubMed:25521849). Decreases enzymatic activity by 60% (PubMed:25037224).
- K318 (= K248) mutation to A: Decreases enzymatic activity by 50%.; mutation to E: Completely abolishes enzymatic activity.
- D341 (= D271) 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 (= D275) 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.
Sites not aligning to the query:
- 18 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
- 108 G→A: Does not bind L-serine and correspondingly no oligomeric transitions is observed in the presence of L-serine.
A0QJI1 Phosphoserine phosphatase; PSP; PSPase; O-phosphoserine phosphohydrolase; EC 3.1.3.3 from Mycobacterium avium (strain 104) (see paper)
45% identity, 66% coverage: 107:314/316 of query aligns to 179:386/411 of A0QJI1
- D187 (= D115) binding
- D189 (= D117) binding
- D343 (= D271) binding
5jlpA Crystal structure of mycobacterium avium serb2 in complex with serine at act domain
45% identity, 66% coverage: 107:314/316 of query aligns to 175:382/396 of 5jlpA
Sites not aligning to the query:
8a21A Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with phenylimidazole (see paper)
45% identity, 66% coverage: 107:314/316 of query aligns to 175:382/396 of 8a21A
- binding magnesium ion: D183 (= D115), D185 (= D117), D339 (= D271)
- binding 4-phenyl-1h-imidazole: D185 (= D117), E192 (= E124), V193 (≠ C125), I194 (= I126), T211 (= T143), M215 (= M147), F221 (= F153), R228 (= R160), G273 (= G205)
Sites not aligning to the query:
8a1zA Crystal structure of phosphoserine phosphatase serb from mycobacterium avium in complex with 1-(2,4-dichlorophenyl)-3-hydroxyurea (see paper)
45% identity, 66% coverage: 107:314/316 of query aligns to 175:382/396 of 8a1zA
- binding 1-(2,4-dichlorophenyl)-3-oxidanyl-urea: D185 (= D117), E192 (= E124), M215 (= M147), F221 (= F153), L225 (= L157), R228 (= R160), G272 (= G204), F274 (= F206), D339 (= D271)
- binding magnesium ion: D183 (= D115), D185 (= D117), D339 (= D271)
1l7oA Crystal structure of phosphoserine phosphatase in apo form (see paper)
40% identity, 64% coverage: 111:313/316 of query aligns to 4:199/200 of 1l7oA
7qplA Crystal structure of phosphoserine phosphatase (serb) from brucella melitensis in complex with phosphate and magnesium
37% identity, 76% coverage: 73:313/316 of query aligns to 49:285/295 of 7qplA
3m1yC Crystal structure of a phosphoserine phosphatase (serb) from helicobacter pylori
37% identity, 65% coverage: 111:315/316 of query aligns to 5:208/208 of 3m1yC
1l8oA Molecular basis for the local conformational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 56% coverage: 112:288/316 of query aligns to 14:193/222 of 1l8oA
Sites not aligning to the query:
1l8lA Molecular basis for the local confomational rearrangement of human phosphoserine phosphatase (see paper)
33% identity, 56% coverage: 112:288/316 of query aligns to 14:193/222 of 1l8lA
- active site: D17 (= D115), V18 (≠ M116), D19 (= D117), G107 (= G204), K155 (= K248), D180 (= D275)
- binding d-2-amino-3-phosphono-propionic acid: D17 (= D115), D19 (= D117), G107 (= G204), K155 (= K248), D176 (= D271), G177 (= G272), T179 (≠ N274)
6hyyA Human phosphoserine phosphatase with serine and phosphate (see paper)
33% identity, 56% coverage: 112:288/316 of query aligns to 13:192/221 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, 56% coverage: 112:288/316 of query aligns to 17:196/225 of P78330
- D20 (= D115) binding
- DVD 20:22 (≠ DMD 115:117) binding
- D22 (= D117) binding
- S23 (= S118) mutation to A: Reduces L-phosphoserine phosphatase activity by about 50%.; mutation to T: Reduces L-phosphoserine phosphatase activity by about 80%.
- E29 (= E124) mutation to D: Reduces L-phosphoserine phosphatase activity by about 95%.; mutation to Q: Loss of L-phosphoserine phosphatase activity.
- D32 (= D127) to N: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894035
- A35 (= A130) to T: in PSPHD; decreased L-phosphoserine phosphatase activity
- M52 (= M147) binding ; to T: in PSPHD; decreased L-phosphoserine phosphatase activity; dbSNP:rs104894036
- G53 (≠ Q148) binding
- R65 (= R160) mutation R->A,K: Loss of L-phosphoserine phosphatase activity.
- SGG 109:111 (= SGG 203:205) binding ; binding
- N133 (= N225) mutation to A: Reduces L-phosphoserine phosphatase activity by about 75%.
- K158 (= K248) binding ; binding
- D179 (= D271) binding
- T182 (≠ N274) binding ; binding ; mutation to S: Reduces L-phosphoserine phosphatase activity by about 99%.; mutation to V: Reduces L-phosphoserine phosphatase activity by about 25%.
Sites not aligning to the query:
- 202 R→A: Reduces L-phosphoserine phosphatase activity by about 99%.; R→K: Reduces L-phosphoserine phosphatase activity by about 95%.
6hyjB Psph human phosphoserine phosphatase (see paper)
33% identity, 56% coverage: 112:288/316 of query aligns to 17:196/223 of 6hyjB
Sites not aligning to the query:
6q6jB Human phosphoserine phosphatase with substrate analogue homo-cysteic acid (see paper)
33% identity, 56% coverage: 112:288/316 of query aligns to 13:192/217 of 6q6jB
- binding calcium ion: D16 (= D115), D18 (= D117), D175 (= D271)
- binding (2~{S})-2-azanyl-4-sulfo-butanoic acid: D16 (= D115), V17 (≠ M116), D18 (= D117), F54 (= F153), S105 (= S203), G106 (= G204), G107 (= G205), K154 (= K248), T178 (≠ N274)
4ap9A Crystal structure of phosphoserine phosphatase from t.Onnurineus in complex with ndsb-201 (see paper)
31% identity, 55% coverage: 113:287/316 of query aligns to 13:174/200 of 4ap9A
- active site: D15 (= D115), I16 (≠ M116), E17 (≠ D117), G103 (= G204), K141 (= K248), D162 (= D275)
- binding 3-pyridinium-1-ylpropane-1-sulfonate: R31 (≠ A131), I32 (≠ M132), T33 (≠ A133), L46 (≠ M147), W52 (≠ F153), D140 (≠ F247), K141 (= K248), Y160 (≠ A273), A161 (≠ N274)
3kd3A Crystal structure of a phosphoserine phosphohydrolase-like protein from francisella tularensis subsp. Tularensis schu s4
28% identity, 54% coverage: 112:281/316 of query aligns to 4:179/216 of 3kd3A
Query Sequence
>6936796 FitnessBrowser__SB2B:6936796
MENTSEYVLQNRLHALATSGQCQLSLYEEGQAPQGERVRLVWATKATEELIFARLAELNC
AAAPLVRRNALSGLELVSKGEGNLSAAFDGIAGLEVLPVTESLPSLRHPGLLVMDMDSTA
IKIECIDELAAMAGVGEAVAEVTERAMQGELDFKQSLRQRVAKLAGADAGIIDTLCARLP
LMDGLTEMLAELKGHGWKLVVASGGFTPFVGHLKATLGLDAAFANELVIADGKLVGEVTG
TVVDANFKADVVSRLGDEYGIKDGQRLAIGDGANDIPMVQRADFGIAFHAKPKLAAAADA
RIHTLDLRVLPFLLQA
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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