SitesBLAST
Comparing N515DRAFT_3581 N515DRAFT_3581 D-3-phosphoglycerate dehydrogenase 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)
63% identity, 100% coverage: 2:410/410 of query aligns to 3:410/410 of P0A9T0
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1ybaA The active form of phosphoglycerate dehydrogenase (see paper)
63% identity, 99% coverage: 4:410/410 of query aligns to 1:406/406 of 1ybaA
- active site: N104 (= N107), R236 (= R239), D260 (= D263), E265 (= E268), H288 (= H291)
- binding 2-oxoglutaric acid: R56 (= R59), S57 (= S60), C79 (= C82), I80 (= I83)
- binding nicotinamide-adenine-dinucleotide: I80 (= I83), F102 (≠ Y105), V108 (= V111), G154 (= G157), G156 (= G159), H157 (= H160), I158 (= I161), Y176 (≠ H179), D177 (= D180), I178 (= I181), K181 (= K184), H206 (= H209), V207 (= V210), P208 (= P211), A234 (= A237), S235 (= S238), R236 (= R239), H288 (= H291), G290 (= G293)
- binding phosphate ion: G81 (= G84), N83 (= N86)
1psdA The allosteric ligand site in the vmax-type cooperative enzyme phosphoglycerate dehydrogenase (see paper)
63% identity, 99% coverage: 7:410/410 of query aligns to 2:404/404 of 1psdA
- active site: N102 (= N107), R234 (= R239), D258 (= D263), E263 (= E268), H286 (= H291)
- binding nicotinamide-adenine-dinucleotide: N102 (= N107), H155 (= H160), I156 (= I161), D175 (= D180), I176 (= I181), K179 (= K184), H204 (= H209), V205 (= V210), P206 (= P211), A232 (= A237), S233 (= S238), R234 (= R239), H286 (= H291)
- binding serine: H338 (= H344), N340 (= N346), R341 (≠ V347), V344 (= V350)
2p9eA Crystal structure of g336v mutant of e.Coli phosphoglycerate dehydrogenase (see paper)
63% identity, 99% coverage: 4:410/410 of query aligns to 1:406/406 of 2p9eA
- active site: N104 (= N107), R236 (= R239), D260 (= D263), E265 (= E268), H288 (= H291)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G156 (= G159), H157 (= H160), I158 (= I161), Y176 (≠ H179), D177 (= D180), I178 (= I181), H206 (= H209), V207 (= V210), P208 (= P211), S212 (≠ A215), A234 (= A237), S235 (= S238), R236 (= R239), H288 (= H291), G290 (= G293)
1sc6D Crystal structure of w139g d-3-phosphoglycerate dehydrogenase complexed with NAD+ (see paper)
60% identity, 99% coverage: 7:410/410 of query aligns to 2:384/384 of 1sc6D
- active site: N102 (= N107), R228 (= R239), D252 (= D263)
- binding nicotinamide-adenine-dinucleotide: P99 (= P104), F100 (≠ Y105), N102 (= N107), T103 (= T108), G146 (= G157), G148 (= G159), H149 (= H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), I170 (= I181), H198 (= H209), V199 (= V210), P200 (= P211), S204 (≠ A215), T205 (= T216), S227 (= S238)
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)
50% identity, 99% coverage: 5:410/410 of query aligns to 51:466/466 of P87228
- S87 (≠ P42) modified: Phosphoserine
- S258 (≠ T213) modified: Phosphoserine
1wwkA Crystal structure of phosphoglycerate dehydrogenase from pyrococcus horikoshii ot3
38% identity, 74% coverage: 10:313/410 of query aligns to 1:300/304 of 1wwkA
- active site: S96 (≠ N107), R230 (= R239), D254 (= D263), E259 (= E268), H278 (= H291)
- binding nicotinamide-adenine-dinucleotide: V100 (= V111), G146 (= G157), F147 (≠ Y158), G148 (= G159), R149 (≠ H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), P170 (≠ I181), V201 (= V210), P202 (= P211), T207 (= T216), T228 (≠ A237), S229 (= S238), D254 (= D263), H278 (= H291), G280 (= G293)
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, 87% coverage: 11:368/410 of query aligns to 8:359/533 of O43175
- T78 (≠ I83) binding
- R135 (≠ K140) 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 160:161) binding
- D175 (= D180) binding
- T207 (≠ V210) binding
- CAR 234:236 (≠ ASR 237:239) binding
- D260 (= D263) binding
- V261 (= V264) 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 (≠ HIGG 291:294) 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
6plgA Crystal structure of human phgdh complexed with compound 15 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/303 of 6plgA
6plfA Crystal structure of human phgdh complexed with compound 1 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 4:300/305 of 6plfA
7dkmA Phgdh covalently linked to oridonin (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 4:300/306 of 7dkmA
- binding nicotinamide-adenine-dinucleotide: T74 (≠ I83), A102 (≠ V111), G148 (= G157), R151 (≠ H160), I152 (= I161), Y170 (≠ H179), D171 (= D180), P172 (vs. gap), I173 (vs. gap), H202 (= H209), T203 (≠ V210), P204 (= P211), T209 (= T216), C230 (≠ A237), A231 (≠ S238), R232 (= R239), H279 (= H291), G281 (= G293)
- binding (1beta,6beta,7beta,8alpha,9beta,10alpha,13alpha,14R,16beta)-1,6,7,14-tetrahydroxy-7,20-epoxykauran-15-one: C14 (≠ S21), K17 (≠ E24), I18 (≠ V25), E293 (≠ I305)
7ewhA Crystal structure of human phgdh in complex with homoharringtonine (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/302 of 7ewhA
- binding (3beta)-O~3~-[(2R)-2,6-dihydroxy-2-(2-methoxy-2-oxoethyl)-6-methylheptanoyl]cephalotaxine: L146 (≠ V156), G147 (= G157), L148 (≠ Y158), G149 (= G159), R150 (≠ H160), I151 (= I161), G152 (= G162), D170 (= D180), H201 (= H209), T202 (≠ V210), P203 (= P211)
6rihA Crystal structure of phgdh in complex with compound 9 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/302 of 6rihA
6rj5A Crystal structure of phgdh in complex with compound 39 (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 3:299/301 of 6rj5A
6cwaA Crystal structure phgdh in complex with nadh and 3-phosphoglycerate at 1.77 a resolution (see paper)
35% identity, 74% coverage: 11:312/410 of query aligns to 2:298/299 of 6cwaA
- binding 1,4-dihydronicotinamide adenine dinucleotide: N96 (= N107), A100 (≠ V111), R149 (≠ H160), I150 (= I161), Y168 (≠ H179), D169 (= D180), P170 (vs. gap), I171 (vs. gap), H200 (= H209), T201 (≠ V210), P202 (= P211), T207 (= T216), C228 (≠ A237), A229 (≠ S238), R230 (= R239), H277 (= H291), G279 (= G293)
6rj3A Crystal structure of phgdh in complex with compound 15 (see paper)
35% identity, 73% coverage: 11:311/410 of query aligns to 2:297/297 of 6rj3A
6rj2A Crystal structure of phgdh in complex with compound 40 (see paper)
35% identity, 73% coverage: 12:312/410 of query aligns to 1:296/299 of 6rj2A
- binding ~{N}-[(1~{R})-1-[4-(ethanoylsulfamoyl)phenyl]ethyl]-2-methyl-5-phenyl-pyrazole-3-carboxamide: G146 (= G159), I148 (= I161), Y166 (≠ H179), D167 (= D180), P168 (vs. gap), I169 (vs. gap), I170 (= I181), H198 (= H209), T199 (≠ V210), L208 (≠ M219), R228 (= R239)
6plfB Crystal structure of human phgdh complexed with compound 1 (see paper)
36% identity, 74% coverage: 11:312/410 of query aligns to 2:290/292 of 6plfB
- binding 4-{(1S)-1-[(5-chloro-6-{[(5S)-2-oxo-1,3-oxazolidin-5-yl]methoxy}-1H-indole-2-carbonyl)amino]-2-hydroxyethyl}benzoic acid: R141 (≠ H160), Y160 (≠ H179), D161 (= D180), P162 (vs. gap), I164 (= I181), L179 (= L196), T193 (≠ V210), P194 (= P211), S198 (≠ A215), L202 (≠ M219)
3ddnB Crystal structure of hydroxypyruvic acid phosphate bound d-3- phosphoglycerate dehydrogenase in mycobacterium tuberculosis (see paper)
38% identity, 68% coverage: 33:311/410 of query aligns to 22:298/525 of 3ddnB
3dc2A Crystal structure of serine bound d-3-phosphoglycerate dehydrogenase from mycobacterium tuberculosis (see paper)
38% identity, 68% coverage: 33:311/410 of query aligns to 21:297/526 of 3dc2A
Sites not aligning to the query:
Query Sequence
>N515DRAFT_3581 N515DRAFT_3581 D-3-phosphoglycerate dehydrogenase
MKTSYPKADIKVLLLEGVSQSAVEVFRRAGYSQIEFHEKSLPEAELKARIAEAHIVGIRS
RSHLTADVLEQARRLIAVGCFCIGTNQVDLETARQQGVPVFNAPYSNTRSVAELVIAEAI
MLLRGIPQKNALCHRGGWTKSAAGSFEVRDKVLGIVGYGHIGTQVGVLAESLGMRVIFHD
IETKLSLGNARAAGSLDDLLERADVVTLHVPETPATKLMIGATELAKMRKGAALINASRG
TVVDIDALAAALRTGHVAGAAVDVFPLEPKGNDDPFVSPLVGMDNVILTPHIGGSTLEAQ
DNIGIEVASKLVRYSDNGSTLSAVNFPEVTLPEHPNSRRLLHIHRNVPGVLSRINELFSA
GNINIDAQFLQTDSQVGYVVIDVSADEAQAGALKDRLAAIPGTLRSRVLY
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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