SitesBLAST
Comparing GFF1729 FitnessBrowser__Phaeo:GFF1729 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)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
50% identity, 100% coverage: 1:395/396 of query aligns to 1:392/394 of 1phpA
- active site: R36 (= R36), K197 (= K197), G351 (= G354), G374 (= G377)
- binding adenosine-5'-diphosphate: G195 (= G195), K201 (= K201), G219 (= G219), G220 (= G220), L237 (= L237), N316 (= N316), P318 (= P318), G320 (= G320), V321 (≠ A321), E323 (= E323), G350 (= G353), D352 (= D355), S353 (≠ T356)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
50% identity, 100% coverage: 1:395/396 of query aligns to 1:392/394 of P18912
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, 97% coverage: 9:394/396 of query aligns to 9:394/654 of P36204
- R36 (= R36) binding
- R118 (= R118) binding
- R151 (= R151) binding
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
48% identity, 97% coverage: 9:394/396 of query aligns to 8:393/398 of 1vpeA
- active site: R35 (= R36), K196 (= K197), G353 (= G354), G376 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G195), A195 (= A196), K196 (= K197), K200 (= K201), G218 (= G219), A219 (≠ G220), N316 (= N316), P318 (= P318), G320 (= G320), V321 (≠ A321), E323 (= E323), G352 (= G353), G353 (= G354), D354 (= D355), S355 (≠ T356)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
47% identity, 99% coverage: 1:394/396 of query aligns to 1:391/394 of P40924
- S183 (≠ G183) modified: Phosphoserine
- T299 (= T299) modified: Phosphothreonine
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
47% identity, 100% coverage: 1:395/396 of query aligns to 1:387/392 of 4feyA
- active site: R36 (= R36), K193 (= K197), G346 (= G354), G369 (= G377)
- binding adenosine-5'-diphosphate: G191 (= G195), S192 (≠ A196), K197 (= K201), G215 (= G219), G316 (= G320), V317 (≠ A321), E319 (= E323), D347 (= D355)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
42% identity, 99% coverage: 4:395/396 of query aligns to 7:417/440 of P07378
16pkA Phosphoglycerate kinase from trypanosoma brucei bisubstrate analog (see paper)
42% identity, 99% coverage: 4:395/396 of query aligns to 3:413/415 of 16pkA
- active site: R35 (= R36), K215 (= K197), G372 (= G354), G395 (= G377)
- binding 1,1,5,5-tetrafluorophosphopentylphosphonic acid adenylate ester: G213 (= G195), A214 (= A196), K219 (= K201), A238 (≠ G220), Y241 (≠ N223), L311 (= L293), P336 (= P318), G338 (= G320), V339 (≠ A321), E341 (= E323), G393 (≠ A375), G394 (= G376), G395 (= G377)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
42% identity, 99% coverage: 4:395/396 of query aligns to 3:413/415 of 13pkA
- active site: R35 (= R36), K215 (= K197), G372 (= G354), G395 (= G377)
- binding adenosine-5'-diphosphate: G213 (= G195), A214 (= A196), K219 (= K201), L311 (= L293), P336 (= P318), G338 (= G320), V339 (≠ A321), E341 (= E323), G371 (= G353), D373 (= D355), S374 (≠ T356)
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
45% identity, 98% coverage: 5:394/396 of query aligns to 4:384/389 of 4ng4B
- active site: R35 (= R36), K191 (= K197), G344 (= G354), G367 (= G377)
- binding adenosine-5'-diphosphate: G189 (= G195), K195 (= K201), G213 (= G219), I286 (= I292), N310 (= N316), G311 (= G317), P312 (= P318), V315 (≠ A321), E317 (= E323), G343 (= G353), D345 (= D355), T346 (= T356)
- binding magnesium ion: D288 (= D294), G314 (= G320), F321 (= F327), S322 (≠ D328), T325 (= T331)
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
45% identity, 98% coverage: 9:395/396 of query aligns to 8:381/386 of 1zmrA
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
45% identity, 98% coverage: 9:395/396 of query aligns to 9:382/387 of P0A799
- K84 (≠ A83) modified: N6-acetyllysine
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
3zlbA Crystal structure of phosphoglycerate kinase from streptococcus pneumoniae (see paper)
44% identity, 97% coverage: 9:394/396 of query aligns to 9:395/398 of 3zlbA
- active site: R36 (= R36), K204 (= K197), G355 (= G354), G378 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G202 (= G195), S203 (≠ A196), G226 (= G219), G227 (= G220), N320 (= N316), P322 (= P318), G324 (= G320), V325 (≠ A321), E327 (= E323), G354 (= G353), G355 (= G354), D356 (= D355), S357 (≠ T356)
Sites not aligning to the query:
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
39% identity, 98% coverage: 7:394/396 of query aligns to 18:421/424 of 1ltkC
- active site: R47 (= R36), K223 (= K197), G381 (= G354), G404 (= G377)
- binding adenosine monophosphate: G221 (= G195), A222 (= A196), K223 (= K197), G245 (= G219), G246 (= G220), G348 (= G320), V349 (≠ A321), E351 (= E323), D382 (= D355)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
40% identity, 98% coverage: 6:394/396 of query aligns to 7:405/408 of 2x15A
- active site: R37 (= R36), K207 (= K197), G365 (= G354), G388 (= G377)
- binding adenosine-5'-diphosphate: G205 (= G195), A206 (= A196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), P330 (= P318), G332 (= G320), V333 (≠ A321), E335 (= E323), G364 (= G353), G365 (= G354), D366 (= D355), T367 (= T356)
- binding adenosine-5'-triphosphate: G205 (= G195), A206 (= A196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), G332 (= G320), V333 (≠ A321), E335 (= E323), G364 (= G353), G365 (= G354), D366 (= D355), T367 (= T356), G387 (= G376), G388 (= G377)
- binding 1,3-bisphosphoglyceric acid: D22 (= D21), N24 (= N23), R37 (= R36), H61 (= H59), R64 (= R62), R121 (= R118), R162 (= R151), K207 (= K197), K211 (= K201), G364 (= G353), G387 (= G376), G388 (= G377)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
40% identity, 98% coverage: 6:394/396 of query aligns to 7:402/405 of 2wzcA
- active site: R37 (= R36), K204 (= K197), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (= A196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (≠ A321), E332 (= E323), G361 (= G353), D363 (= D355), T364 (= T356)
- binding tetrafluoroaluminate ion: R37 (= R36), K204 (= K197), K208 (= K201), G361 (= G353), G362 (= G354), G384 (= G376)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
40% identity, 98% coverage: 6:394/396 of query aligns to 7:402/405 of 2wzbA
- active site: R37 (= R36), K204 (= K197), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (= A196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (≠ A321), E332 (= E323), G361 (= G353), D363 (= D355), T364 (= T356)
- binding trifluoromagnesate: K204 (= K197), K208 (= K201), G361 (= G353), G384 (= G376), G385 (= G377)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
40% identity, 98% coverage: 6:394/396 of query aligns to 9:414/417 of 4o33A
- active site: R39 (= R36), K216 (= K197), G374 (= G354), G397 (= G377)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G219), G239 (= G220), T255 (≠ K235), L257 (= L237), F292 (= F272), M312 (= M291), G313 (≠ I292), L314 (= L293), G341 (= G320), V342 (≠ A321)
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
40% identity, 98% coverage: 6:394/396 of query aligns to 8:413/416 of 5m1rA
- active site: R38 (= R36), K215 (= K197), G373 (= G354), G396 (= G377)
- binding adenosine-5'-diphosphate: G213 (= G195), A214 (= A196), K219 (= K201), G237 (= G219), G238 (= G220), L256 (= L237), G340 (= G320), V341 (≠ A321), E343 (= E323), D374 (= D355), T375 (= T356)
- binding magnesium ion: R150 (≠ A131), A151 (= A132), G372 (= G353), T375 (= T356)
2y3iA The structure of the fully closed conformation of human pgk in complex with l-adp, 3pg and the tsa aluminium tetrafluoride (see paper)
40% identity, 98% coverage: 6:394/396 of query aligns to 7:412/414 of 2y3iA
- active site: R37 (= R36), K214 (= K197), G372 (= G354), G395 (= G377)
- binding tetrafluoroaluminate ion: K214 (= K197), G371 (= G353), G372 (= G354), G394 (= G376)
- binding l-adenosine-5'-diphosphate: G212 (= G195), A213 (= A196), F290 (= F272), N335 (= N316), G339 (= G320), V340 (≠ A321), E342 (= E323), G371 (= G353), G372 (= G354), D373 (= D355), T374 (= T356)
Query Sequence
>GFF1729 FitnessBrowser__Phaeo:GFF1729
MGWNALDTMDLAGKRVLVRVDINVPVEDGRVTDDTRIQRVAPTIKDILAAGGTPILLAHF
GRPKGKVVAEMSLRPLVPALEAAFGAPVTFAADCRGPAAEAAVQGLPAGGVLLLENTRFH
AGEEKNDTDLAAEMAKLGDIYCNDAFSAAHRAHASTEALARLLPACAGRLMQAELTALET
ALGQPQRPVTAVVGGAKVSTKLELLGNLVGKVDNLVIGGGMANTFLAAQGIDVGKSLCEH
DMADTAREILSKAEDQGCKIILPVDVVVAREFKAGADNETVAADACPADAMILDAGPQTV
AAVADTLSTSKTLIWNGPMGAFEIAPFDAATNAAAQQAASLTKSGALVSVAGGGDTVAAL
NQAGAAADFTYISTAGGAFLEWMEGKTLPGVAALEG
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