SitesBLAST
Comparing 351200 BT1672 phosphoglycerate kinase (NCBI ptt file) 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)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
49% identity, 100% coverage: 2:419/419 of query aligns to 4:393/394 of 1phpA
- active site: R36 (= R35), K197 (= K221), G351 (= G377), G374 (= G400)
- binding adenosine-5'-diphosphate: G195 (= G219), K201 (= K225), G219 (= G243), G220 (= G244), L237 (≠ I261), N316 (= N340), P318 (= P342), G320 (= G344), V321 (= V345), E323 (= E347), G350 (= G376), D352 (= D378), S353 (= S379)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
49% identity, 100% coverage: 2:419/419 of query aligns to 4:393/394 of P18912
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
48% identity, 100% coverage: 2:419/419 of query aligns to 4:393/394 of P40924
- S183 (≠ N207) modified: Phosphoserine
- T299 (= T323) modified: Phosphothreonine
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
47% identity, 99% coverage: 3:418/419 of query aligns to 4:394/398 of 1vpeA
- active site: R35 (= R35), K196 (= K221), G353 (= G377), G376 (= G400)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G219), A195 (≠ S220), K196 (= K221), K200 (= K225), G218 (= G243), A219 (≠ G244), N316 (= N340), P318 (= P342), G320 (= G344), V321 (= V345), E323 (= E347), G352 (= G376), G353 (= G377), D354 (= D378), S355 (= S379)
P36204 Bifunctional PGK/TIM; EC 2.7.2.3; EC 5.3.1.1 from Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) (see paper)
48% identity, 99% coverage: 3:417/419 of query aligns to 5:394/654 of P36204
- R36 (= R35) binding
- R118 (= R116) binding
- R151 (= R172) binding
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
47% identity, 100% coverage: 3:419/419 of query aligns to 8:414/416 of P00560
- R22 (= R17) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R35) binding
- R122 (= R116) binding
- R169 (= R172) binding
1qpgA 3-phosphoglycerate kinase, mutation r65q (see paper)
47% identity, 100% coverage: 3:419/419 of query aligns to 7:413/415 of 1qpgA
- active site: R38 (= R35), K213 (= K221), G371 (= G377), G394 (= G400)
- binding magnesium-5'-adenyly-imido-triphosphate: G235 (= G243), G236 (= G244), N334 (= N340), P336 (= P342), G338 (= G344), V339 (= V345), F340 (= F346), E341 (= E347), G370 (= G376), G371 (= G377), D372 (= D378), T373 (≠ S379)
3pgkA The structure of yeast phosphoglycerate kinase at 0.25 nm resolution (see paper)
47% identity, 100% coverage: 3:419/419 of query aligns to 7:413/415 of 3pgkA
- active site: R38 (= R35), K213 (= K221), G371 (= G377), G394 (= G400)
- binding adenosine-5'-triphosphate: G211 (= G219), A212 (≠ S220), K213 (= K221), F289 (= F296), L311 (= L317), N334 (= N340), G335 (= G341), P336 (= P342), G338 (= G344), V339 (= V345), D372 (= D378)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
48% identity, 97% coverage: 12:417/419 of query aligns to 25:421/424 of 1ltkC
- active site: R47 (= R35), K223 (= K221), G381 (= G377), G404 (= G400)
- binding adenosine monophosphate: G221 (= G219), A222 (≠ S220), K223 (= K221), G245 (= G243), G246 (= G244), G348 (= G344), V349 (= V345), E351 (= E347), D382 (= D378)
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
47% identity, 97% coverage: 11:418/419 of query aligns to 16:414/416 of 6yjeA
- active site: R39 (= R35), K215 (= K221), G373 (= G377), G396 (= G400)
- binding (2~{S})-2-(5-nitrofuran-2-yl)-2,3,5,6,7,8-hexahydro-1~{H}-[1]benzothiolo[2,3-d]pyrimidin-4-one: G237 (= G243), G238 (= G244), Y241 (= Y247), L256 (≠ I261), F291 (= F296), M311 (≠ E315), G312 (= G316), L313 (= L317), G340 (= G344), V341 (= V345)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
43% identity, 99% coverage: 3:418/419 of query aligns to 7:414/416 of 1kf0A
P00558 Phosphoglycerate kinase 1; Cell migration-inducing gene 10 protein; Primer recognition protein 2; PRP 2; EC 2.7.2.3 from Homo sapiens (Human) (see 16 papers)
44% identity, 99% coverage: 3:418/419 of query aligns to 8:415/417 of P00558
- DFN 24:26 (= DFN 19:21) binding
- R39 (= R35) binding
- HLGR 63:66 (= HLGR 58:61) binding
- L88 (= L81) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ N90) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R116) binding
- K131 (= K124) modified: N6-malonyllysine; alternate
- G158 (≠ A159) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D165) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R172) binding
- K191 (≠ E196) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R211) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K221) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K225) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (≠ K256) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ A270) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (= D272) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D289) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (= G316) binding
- D315 (= D318) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I319) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ I326) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E347) binding
- T352 (≠ S355) to N: in dbSNP:rs137852530
- GGDT 373:376 (≠ GGDS 376:379) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
44% identity, 99% coverage: 3:418/419 of query aligns to 6:413/414 of 2y3iA
- active site: R37 (= R35), K214 (= K221), G372 (= G377), G395 (= G400)
- binding tetrafluoroaluminate ion: K214 (= K221), G371 (= G376), G372 (= G377), G394 (= G399)
- binding l-adenosine-5'-diphosphate: G212 (= G219), A213 (≠ S220), F290 (= F296), N335 (= N340), G339 (= G344), V340 (= V345), E342 (= E347), G371 (= G376), G372 (= G377), D373 (= D378), T374 (≠ S379)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
43% identity, 99% coverage: 3:418/419 of query aligns to 6:406/408 of 2x15A
- active site: R37 (= R35), K207 (= K221), G365 (= G377), G388 (= G400)
- binding adenosine-5'-diphosphate: G205 (= G219), A206 (≠ S220), K207 (= K221), K211 (= K225), G229 (= G243), G230 (= G244), N328 (= N340), P330 (= P342), G332 (= G344), V333 (= V345), E335 (= E347), G364 (= G376), G365 (= G377), D366 (= D378), T367 (≠ S379)
- binding adenosine-5'-triphosphate: G205 (= G219), A206 (≠ S220), K207 (= K221), K211 (= K225), G229 (= G243), G230 (= G244), N328 (= N340), G332 (= G344), V333 (= V345), E335 (= E347), G364 (= G376), G365 (= G377), D366 (= D378), T367 (≠ S379), G387 (= G399), G388 (= G400)
- binding 1,3-bisphosphoglyceric acid: D22 (= D19), N24 (= N21), R37 (= R35), H61 (= H58), R64 (= R61), R121 (= R116), R162 (= R172), K207 (= K221), K211 (= K225), G364 (= G376), G387 (= G399), G388 (= G400)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
44% identity, 99% coverage: 3:418/419 of query aligns to 8:415/417 of 4o33A
- active site: R39 (= R35), K216 (= K221), G374 (= G377), G397 (= G400)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G243), G239 (= G244), T255 (≠ I259), L257 (≠ I261), F292 (= F296), M312 (≠ E315), G313 (= G316), L314 (= L317), G341 (= G344), V342 (= V345)
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
43% identity, 99% coverage: 3:418/419 of query aligns to 6:405/407 of 4axxA
- active site: R37 (= R35), K206 (= K221), G364 (= G377), G387 (= G400)
- binding adenosine-5'-diphosphate: G204 (= G219), A205 (≠ S220), K210 (= K225), G228 (= G243), G229 (= G244), N327 (= N340), P329 (= P342), G331 (= G344), V332 (= V345), E334 (= E347), G363 (= G376), G364 (= G377), D365 (= D378), T366 (≠ S379)
- binding beryllium trifluoride ion: K206 (= K221), K210 (= K225), G363 (= G376)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
42% identity, 99% coverage: 3:418/419 of query aligns to 8:415/417 of P09041
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
43% identity, 99% coverage: 3:418/419 of query aligns to 7:414/416 of 1vjcA
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
44% identity, 99% coverage: 3:418/419 of query aligns to 7:414/416 of 5m1rA
- active site: R38 (= R35), K215 (= K221), G373 (= G377), G396 (= G400)
- binding adenosine-5'-diphosphate: G213 (= G219), A214 (≠ S220), K219 (= K225), G237 (= G243), G238 (= G244), L256 (≠ I261), G340 (= G344), V341 (= V345), E343 (= E347), D374 (= D378), T375 (≠ S379)
- binding magnesium ion: R150 (≠ T152), A151 (≠ K153), G372 (= G376), T375 (≠ S379)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
43% identity, 99% coverage: 3:418/419 of query aligns to 6:403/405 of 2wzcA
- active site: R37 (= R35), K204 (= K221), G362 (= G377), G385 (= G400)
- binding adenosine-5'-diphosphate: G202 (= G219), A203 (≠ S220), K204 (= K221), K208 (= K225), G226 (= G243), G227 (= G244), N325 (= N340), P327 (= P342), G329 (= G344), V330 (= V345), E332 (= E347), G361 (= G376), D363 (= D378), T364 (≠ S379)
- binding tetrafluoroaluminate ion: R37 (= R35), K204 (= K221), K208 (= K225), G361 (= G376), G362 (= G377), G384 (= G399)
Query Sequence
>351200 BT1672 phosphoglycerate kinase (NCBI ptt file)
MQTIDKFNFAGKKAFVRVDFNVPLDENFNITDDTRMRAALPTLKKILADGGSIIIGSHLG
RPKGVADKFSLKHIIKHLSELLGVEVQFANDCMGEEAAVKAAALQPGEVLLLENLRFYAE
EEGKPRGLAEDATDEEKAAAKKAVKESQKEFTKKLASYADCYVNDAFGTAHRAHASTALI
AKYFDTDNKMFGYLMEKEVKAVDKVLNDIQRPFTAIMGGSKVSSKIEIIENLLNKVDNLI
IAGGMTYTFTKAMGGKIGISICEDDKLDLALDLIKKAKEKGVNLVLAVDAKIADAFSNDA
NTQFCAVDEIPDGWEGLDIGPKTEEIFANVIKESKTILWNGPTGVFEFENFTHGSRTVGE
AIVEATKNGAFSLVGGGDSVACVNKFGLASGVSYVSTGGGALLEAIEGKVLPGIAAINE
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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