SitesBLAST
Comparing 5210768 FitnessBrowser__PV4:5210768 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)
P0A9T0 D-3-phosphoglycerate dehydrogenase; PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Escherichia coli (strain K12) (see 2 papers)
69% identity, 100% coverage: 1:409/409 of query aligns to 1:410/410 of P0A9T0
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
69% identity, 99% coverage: 5:409/409 of query aligns to 1:406/406 of 1ybaA
- active site: N104 (= N108), R236 (= R240), D260 (= D264), E265 (= E269), H288 (= H292)
- binding 2-oxoglutaric acid: R56 (= R60), S57 (= S61), C79 (= C83), I80 (= I84)
- binding nicotinamide-adenine-dinucleotide: I80 (= I84), F102 (= F106), V108 (= V112), G154 (= G158), G156 (= G160), H157 (= H161), I158 (= I162), Y176 (≠ F180), D177 (= D181), I178 (= I182), K181 (= K185), H206 (= H210), V207 (= V211), P208 (= P212), A234 (= A238), S235 (= S239), R236 (= R240), H288 (= H292), G290 (= G294)
- binding phosphate ion: G81 (= G85), N83 (= N87)
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
69% identity, 99% coverage: 7:409/409 of query aligns to 1:404/404 of 1psdA
- active site: N102 (= N108), R234 (= R240), D258 (= D264), E263 (= E269), H286 (= H292)
- binding nicotinamide-adenine-dinucleotide: N102 (= N108), H155 (= H161), I156 (= I162), D175 (= D181), I176 (= I182), K179 (= K185), H204 (= H210), V205 (= V211), P206 (= P212), A232 (= A238), S233 (= S239), R234 (= R240), H286 (= H292)
- binding serine: H338 (= H345), N340 (= N347), R341 (= R348), V344 (≠ I351)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
69% identity, 99% coverage: 5:409/409 of query aligns to 1:406/406 of 2p9eA
- active site: N104 (= N108), R236 (= R240), D260 (= D264), E265 (= E269), H288 (= H292)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G160), H157 (= H161), I158 (= I162), Y176 (≠ F180), D177 (= D181), I178 (= I182), H206 (= H210), V207 (= V211), P208 (= P212), S212 (≠ Q216), A234 (= A238), S235 (= S239), R236 (= R240), H288 (= H292), G290 (= G294)
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
65% identity, 99% coverage: 7:409/409 of query aligns to 1:384/384 of 1sc6D
- active site: N102 (= N108), R228 (= R240), D252 (= D264)
- binding nicotinamide-adenine-dinucleotide: P99 (= P105), F100 (= F106), N102 (= N108), T103 (= T109), G146 (= G158), G148 (= G160), H149 (= H161), I150 (= I162), Y168 (≠ F180), D169 (= D181), I170 (= I182), H198 (= H210), V199 (= V211), P200 (= P212), S204 (≠ Q216), T205 (= T217), S227 (= S239)
P87228 Putative D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; EC 1.1.1.95; EC 1.1.1.399 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
51% identity, 98% coverage: 9:409/409 of query aligns to 54:466/466 of P87228
- S87 (≠ G43) modified: Phosphoserine
- S258 (≠ T214) modified: Phosphoserine
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
39% identity, 74% coverage: 11:314/409 of query aligns to 1:300/304 of 1wwkA
- active site: S96 (≠ N108), R230 (= R240), D254 (= D264), E259 (= E269), H278 (= H292)
- binding nicotinamide-adenine-dinucleotide: V100 (= V112), G146 (= G158), F147 (≠ Y159), G148 (= G160), R149 (≠ H161), I150 (= I162), Y168 (≠ F180), D169 (= D181), P170 (= P187), V201 (= V211), P202 (= P212), T207 (= T217), T228 (≠ A238), S229 (= S239), D254 (= D264), H278 (= H292), G280 (= G294)
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 3:295/301 of 6rj5A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 2:294/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N108), A100 (≠ V112), R149 (≠ H161), I150 (= I162), Y168 (≠ F180), D169 (= D181), P170 (vs. gap), I171 (vs. gap), H200 (= H210), T201 (≠ V211), P202 (= P212), T207 (= T217), C228 (≠ A238), A229 (≠ S239), R230 (= R240), H277 (= H292), G279 (= G294)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 3:295/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ I157), G147 (= G158), L148 (≠ Y159), G149 (= G160), R150 (≠ H161), I151 (= I162), G152 (= G163), D170 (= D181), H201 (= H210), T202 (≠ V211), P203 (= P212)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 3:295/302 of 6rihA
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 3:295/303 of 6plgA
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 4:296/305 of 6plfA
7dkmA Phgdh covalently linked to oridonin (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 4:296/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ I84), A102 (≠ V112), G148 (= G158), R151 (≠ H161), I152 (= I162), Y170 (≠ F180), D171 (= D181), P172 (vs. gap), I173 (vs. gap), H202 (= H210), T203 (≠ V211), P204 (= P212), T209 (= T217), C230 (≠ A238), A231 (≠ S239), R232 (= R240), H279 (= H292), G281 (= G294)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ S22), K17 (≠ D25), I18 (≠ V26), E293 (≠ I306)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
34% identity, 73% coverage: 12:309/409 of query aligns to 2:294/297 of 6rj3A
O43175 D-3-phosphoglycerate dehydrogenase; 3-PGDH; 2-oxoglutarate reductase; Malate dehydrogenase; EC 1.1.1.95; EC 1.1.1.399; EC 1.1.1.37 from Homo sapiens (Human) (see 3 papers)
33% identity, 77% coverage: 12:326/409 of query aligns to 8:317/533 of O43175
- T78 (≠ I84) binding
- R135 (≠ K141) to W: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606949
- RI 155:156 (≠ HI 161:162) binding
- D175 (= D181) binding
- T207 (≠ V211) binding
- CAR 234:236 (≠ ASR 238:240) binding
- D260 (= D264) binding
- V261 (= V265) to M: in PHGDHD; results in a four-fold decrease in substrate affinity and a slight increase in maximal enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs267606947
- HLGA 283:286 (≠ HVGG 292:295) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 373 A → T: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs201553627
- 377 G → S: in PHGDHD; results in a 2-fold decrease in enzyme activity with 3-phosphohydroxypyruvate, but no change in substrate affinity; dbSNP:rs267606948
- 425 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907988
- 490 V → M: in PHGDHD; results in almost undetectable enzyme activity with 3-phosphohydroxypyruvate; dbSNP:rs121907987
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
34% identity, 73% coverage: 13:309/409 of query aligns to 1:292/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G160), I148 (= I162), Y166 (≠ F180), D167 (= D181), P168 (vs. gap), I169 (vs. gap), I170 (= I182), H198 (= H210), T199 (≠ V211), L208 (≠ M220), R228 (= R240)
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
38% identity, 65% coverage: 45:309/409 of query aligns to 33:294/526 of 3dc2A
Sites not aligning to the query:
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
38% identity, 65% coverage: 45:309/409 of query aligns to 34:295/525 of 3ddnB
2eklA Structure of st1218 protein from sulfolobus tokodaii
35% identity, 72% coverage: 11:305/409 of query aligns to 5:295/312 of 2eklA
- active site: S100 (≠ N108), R232 (= R240), D256 (= D264), E261 (= E269), H282 (= H292)
- binding nicotinamide-adenine-dinucleotide: I76 (= I84), S100 (≠ N108), G148 (= G158), G150 (= G160), R151 (≠ H161), I152 (= I162), Y170 (≠ F180), D171 (= D181), I172 (= I182), L173 (≠ E183), H202 (= H210), V203 (= V211), T204 (≠ P212), I212 (≠ M220), T230 (≠ A238), S231 (= S239), D256 (= D264), G284 (= G294)
Query Sequence
>5210768 FitnessBrowser__PV4:5210768
MAKHSLDKDKIKILLLEGVHQSAVDVFKRAGYNNIEYHKASLGEEELLASIKDAHFVGIR
SRTQLTKAVLDKAEKLVSIGCFCIGTNQVDLAAAEKLGIPVFNAPFSNTRSVAELVLGEI
IMLLRGIPQRNALAHRGGWLKSANGSFEARGKTLGVIGYGHIGTQLGILAETLGMRVIFF
DIEDKLPLGNAQQIHSLEQLLSLADVVSLHVPETPQTKNMIGSKELAAMRQGSILINASR
GTVVDIDALAEAIRGDHIVGAAIDVFPVEPKSNDDEFVSPLRGLDNVLLTPHVGGSTQEA
QENIGIEVAGKLAKYSDNGSTMTAVNFPEVSLAQHKDTSRLLHIHHNRPGILIKINQAFA
EKGINIAAQYLQTTAEIGYVVMEVNSDQADEALEEMKAIDGTIRTRLLH
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