SitesBLAST
Comparing Pf1N1B4_4257 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4257 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)
1pwhA Rat liver l-serine dehydratase- complex with pyridoxyl-(o-methyl- serine)-5-monophosphate (see paper)
44% identity, 97% coverage: 2:303/310 of query aligns to 7:320/327 of 1pwhA
- active site: K41 (= K35), A65 (≠ G59), E194 (= E186), A198 (= A190), S200 (= S192), A222 (≠ S214), A269 (= A261), C303 (= C287)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-o-methyl-l-serine: F40 (= F34), K41 (= K35), S64 (= S58), A65 (≠ G59), N67 (= N61), A68 (= A62), F136 (= F129), G168 (= G160), G169 (= G161), G170 (= G162), G171 (= G163), A222 (≠ S214), G224 (= G216), C303 (= C287), G304 (= G288)
Q8VBT2 L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Mus musculus (Mouse)
44% identity, 96% coverage: 2:298/310 of query aligns to 7:315/327 of Q8VBT2
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
Q96GA7 Serine dehydratase-like; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; TDH; Serine dehydratase 2; SDH 2; EC 4.3.1.19; EC 4.3.1.17 from Homo sapiens (Human) (see paper)
43% identity, 95% coverage: 2:295/310 of query aligns to 14:317/329 of Q96GA7
- G72 (= G59) mutation to A: Strongly increased enzyme activity towards threonine.
- C309 (= C287) mutation to A: Loss of enzyme activity.
2rkbA Serine dehydratase like-1 from human cancer cells (see paper)
43% identity, 95% coverage: 2:295/310 of query aligns to 4:307/318 of 2rkbA
- active site: K38 (= K35), G62 (= G59), E190 (= E186), A194 (= A190), C196 (≠ S192), S218 (= S214), A265 (= A261), C299 (= C287)
- binding pyridoxal-5'-phosphate: F37 (= F34), K38 (= K35), N64 (= N61), G164 (≠ S158), G165 (≠ V159), G166 (= G160), G167 (= G161), S218 (= S214), C299 (= C287)
P09367 L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Rattus norvegicus (Rat) (see paper)
39% identity, 97% coverage: 2:303/310 of query aligns to 7:356/363 of P09367
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
P20132 L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Homo sapiens (Human) (see paper)
42% identity, 96% coverage: 2:298/310 of query aligns to 7:315/328 of P20132
- C303 (= C287) mutation to A: Loss of enzyme activity.
1p5jA Crystal structure analysis of human serine dehydratase (see paper)
42% identity, 96% coverage: 2:298/310 of query aligns to 4:312/319 of 1p5jA
- active site: K38 (= K35), A62 (≠ G59), E191 (= E186), A195 (= A190), S197 (= S192), A219 (≠ S214), C300 (= C287)
- binding pyridoxal-5'-phosphate: F37 (= F34), K38 (= K35), N64 (= N61), V164 (= V159), G165 (= G160), G166 (= G161), G167 (= G162), G168 (= G163), A219 (≠ S214), C300 (= C287), G301 (= G288), G302 (= G289)
5c3uA Crystal structure of a fungal l-serine ammonia-lyase from rhizomucor miehei (see paper)
36% identity, 94% coverage: 2:293/310 of query aligns to 3:303/315 of 5c3uA
- active site: K37 (= K35), G63 (= G59), E191 (= E186), S195 (≠ A190), A197 (≠ S192), S219 (= S214), T297 (≠ C287)
- binding pyridoxal-5'-phosphate: K37 (= K35), N65 (= N61), S132 (≠ F129), P163 (≠ T157), G165 (≠ V159), G166 (= G160), G167 (= G161), G168 (= G162), S219 (= S214), T297 (≠ C287)
1tdjA Threonine deaminase (biosynthetic) from e. Coli (see paper)
33% identity, 85% coverage: 6:267/310 of query aligns to 28:290/494 of 1tdjA
- active site: K58 (= K35), A83 (≠ G59), E209 (= E186), S213 (≠ A190), C215 (≠ S192), G237 (≠ S214)
- binding pyridoxal-5'-phosphate: F57 (= F34), K58 (= K35), N85 (= N61), G184 (= G160), G185 (= G161), G186 (= G162), G187 (= G163), G237 (≠ S214), E282 (= E259)
Sites not aligning to the query:
P04968 L-threonine dehydratase biosynthetic IlvA; Threonine deaminase; EC 4.3.1.19 from Escherichia coli (strain K12) (see paper)
33% identity, 85% coverage: 6:267/310 of query aligns to 32:294/514 of P04968
- K62 (= K35) modified: N6-(pyridoxal phosphate)lysine
- N89 (= N61) binding
- GGGGL 188:192 (= GGGGL 160:164) binding
Sites not aligning to the query:
7nbhAAA structure of human serine racemase in complex with DSiP fragment Z26781964, XChem fragment screen (see paper)
29% identity, 96% coverage: 2:300/310 of query aligns to 14:320/320 of 7nbhAAA
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding N-[(1H-benzimidazol-2-yl)methyl]furan-2-carboxamide: S81 (≠ G59), G85 (= G63), Q86 (≠ L64), K111 (≠ T89), I115 (= I93), Y118 (≠ T96), D235 (= D209), P281 (= P260), N313 (≠ S293), V314 (≠ A294), D315 (≠ Q295)
7nbgAAA structure of human serine racemase in complex with DSiP fragment Z52314092, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:312/322 of 7nbgAAA
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N83 (= N61), G182 (= G160), G183 (= G161), G184 (= G162), G185 (= G163), M186 (≠ L164), G236 (≠ T210), V237 (= V211), T282 (≠ A261), S310 (≠ C287), G311 (= G288)
- binding ~{N}-[2-(2-methylphenyl)ethyl]ethanamide: S81 (≠ G59), G85 (= G63), Q86 (≠ L64), I101 (= I79), K111 (≠ T89), I115 (= I93), Y118 (≠ T96)
7nbfAAA structure of human serine racemase in complex with DSiP fragment Z126932614, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:312/323 of 7nbfAAA
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding magnesium ion: N244 (≠ A221)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N83 (= N61), G182 (= G160), G183 (= G161), G184 (= G162), G185 (= G163), M186 (≠ L164), G236 (≠ T210), V237 (= V211), T282 (≠ A261), S310 (≠ C287), G311 (= G288)
- binding 2-[(methylsulfonyl)methyl]-1H-benzimidazole: H21 (≠ I9), L22 (= L10), T23 (≠ H11), P24 (= P12), L26 (= L14), T27 (≠ S15), F46 (≠ L28)
Sites not aligning to the query:
7nbdAAA structure of human serine racemase in complex with DSiP fragment Z235449082, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:312/323 of 7nbdAAA
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding [4-(1H-benzimidazol-1-yl)phenyl]methanol: W272 (≠ A251), L278 (= L257)
- binding magnesium ion: N244 (≠ A221)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N83 (= N61), G182 (= G160), G183 (= G161), G184 (= G162), G185 (= G163), M186 (≠ L164), G236 (≠ T210), V237 (= V211), E280 (= E259), T282 (≠ A261), S310 (≠ C287), G311 (= G288)
Sites not aligning to the query:
7nbcCCC structure of human serine racemase in complex with DSiP fragment Z2856434779, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:312/323 of 7nbcCCC
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding biphenyl-4-ylacetic acid: T78 (≠ C56), H79 (≠ P57), H84 (≠ A62), V148 (= V126), H149 (≠ P127), P150 (≠ A128)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N83 (= N61), G182 (= G160), G183 (= G161), G184 (= G162), G185 (= G163), M186 (≠ L164), G236 (≠ T210), V237 (= V211), T282 (≠ A261), S310 (≠ C287), G311 (= G288)
7nbcAAA structure of human serine racemase in complex with DSiP fragment Z2856434779, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:312/323 of 7nbcAAA
- active site: K53 (= K35), S81 (≠ G59), E207 (= E186), A211 (= A190), D213 (≠ S192), G236 (≠ T210), L309 (≠ V286), S310 (≠ C287)
- binding calcium ion: E207 (= E186), A211 (= A190), D213 (≠ S192)
- binding magnesium ion: N244 (≠ A221)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N83 (= N61), G182 (= G160), G183 (= G161), G184 (= G162), G185 (= G163), M186 (≠ L164), G236 (≠ T210), V237 (= V211), T282 (≠ A261), S310 (≠ C287), G311 (= G288)
Sites not aligning to the query:
3l6bA X-ray crystal structure of human serine racemase in complex with malonate a potent inhibitor (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 15:308/322 of 3l6bA
- active site: K54 (= K35), S77 (≠ G59), E203 (= E186), A207 (= A190), D209 (≠ S192), G232 (≠ T210), T278 (≠ A261), L305 (≠ V286), S306 (≠ C287)
- binding malonate ion: K54 (= K35), S76 (= S58), S77 (≠ G59), N79 (= N61), H80 (≠ A62), R128 (≠ N111), G232 (≠ T210)
- binding manganese (ii) ion: E203 (= E186), A207 (= A190), D209 (≠ S192)
- binding pyridoxal-5'-phosphate: F53 (= F34), K54 (= K35), N79 (= N61), G178 (= G160), G179 (= G161), G180 (= G162), G181 (= G163), M182 (≠ L164), V233 (= V211), E276 (= E259), T278 (≠ A261), S306 (≠ C287), G307 (= G288)
7nbgDDD structure of human serine racemase in complex with DSiP fragment Z52314092, XChem fragment screen (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:307/310 of 7nbgDDD
- active site: K53 (= K35), S76 (≠ G59), E202 (= E186), A206 (= A190), D208 (≠ S192), G231 (≠ T210), L304 (≠ V286), S305 (≠ C287)
- binding calcium ion: E202 (= E186), A206 (= A190), D208 (≠ S192)
- binding magnesium ion: N239 (≠ A221)
- binding ortho-xylene: S76 (≠ G59), Q81 (≠ L64), I96 (= I79), Y113 (≠ T96)
- binding pyridoxal-5'-phosphate: F52 (= F34), K53 (= K35), N78 (= N61), G177 (= G160), G178 (= G161), G179 (= G162), G180 (= G163), M181 (≠ L164), G231 (≠ T210), V232 (= V211), E275 (= E259), T277 (≠ A261), S305 (≠ C287), G306 (= G288)
Sites not aligning to the query:
6zspAAA serine racemase bound to atp and malonate. (see paper)
29% identity, 93% coverage: 2:289/310 of query aligns to 14:305/320 of 6zspAAA
- active site: K53 (= K35), S74 (≠ G59), E200 (= E186), A204 (= A190), D206 (≠ S192), G229 (≠ T210), L302 (≠ V286), S303 (≠ C287)
- binding adenosine-5'-triphosphate: S28 (≠ T16), S29 (≠ P17), I30 (vs. gap), K48 (≠ P30), T49 (≠ S31), Q79 (≠ L64), Y111 (≠ T96), E266 (≠ N252), R267 (≠ D253), K269 (≠ R255)
- binding magnesium ion: E200 (= E186), A204 (= A190), D206 (≠ S192)
- binding malonate ion: K53 (= K35), S73 (= S58), S74 (≠ G59), N76 (= N61), H77 (≠ A62), R125 (≠ N111), G229 (≠ T210), S232 (≠ T213)
Sites not aligning to the query:
Q7XSN8 Serine racemase; D-serine dehydratase; D-serine ammonia-lyase; L-serine dehydratase; L-serine ammonia-lyase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Oryza sativa subsp. japonica (Rice) (see paper)
29% identity, 87% coverage: 19:289/310 of query aligns to 52:325/339 of Q7XSN8
- E219 (= E186) mutation to A: Reduces catalytic activity and abolishes the regulatory effect of Mg(2+) addition; when associated with A-225.
- D225 (≠ S192) mutation to A: Reduces catalytic activity and abolishes the regulatory effect of Mg(2+) addition; when associated with A-219.
Query Sequence
>Pf1N1B4_4257 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_4257
MLHIRTPLILHPGLSTPARRIWLKLENLQPSGSFKLRGMGLLCSQAAEQGKRKVVCPSGG
NAGLATAVAAASLGLKACIVVPNTTPETTRARIRKTGAEVIVHGKVWDEANQRAKELAKG
ADTEYVPAFDHPVLWEGHSTMIDEILEDCPQVDVLVTSVGGGGLLAGLLTGLIRHQRMDC
RIVACETRGAASFAAAISAGHPVRLPRIDTVATSLGAAQVAAWPVQHILDFAHECVVLSD
DEAIMGVVRYANDLRQLVEPACGVSLAVAYLDHPAIAEAHDVVIVVCGGVSISAQLVAGW
ARLSAGAQAT
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