SitesBLAST
Comparing CCNA_03359 FitnessBrowser__Caulo:CCNA_03359 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)
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)
49% identity, 99% coverage: 1:394/396 of query aligns to 1:394/654 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)
49% identity, 98% coverage: 5:394/396 of query aligns to 4:393/398 of 1vpeA
- active site: R35 (= R36), K196 (= K197), G353 (= G354), G376 (= G377)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G195), A195 (≠ S196), K196 (= K197), K200 (= K201), G218 (= G219), A219 (≠ G220), N316 (= N316), P318 (= P318), G320 (= G320), V321 (= V321), E323 (= E323), G352 (= G353), G353 (= G354), D354 (= D355), S355 (≠ T356)
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 (= V321), 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
4feyA An x-ray structure of a putative phosphogylcerate kinase with bound adp from francisella tularensis subsp. Tularensis schu s4
46% 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 (= S196), K197 (= K201), G215 (= G219), G316 (= G320), V317 (= V321), E319 (= E323), D347 (= D355)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
46% identity, 99% coverage: 1:394/396 of query aligns to 1:391/394 of P40924
- S183 (≠ G183) modified: Phosphoserine
- T299 (≠ S299) modified: Phosphothreonine
4ng4B Structure of phosphoglycerate kinase (cbu_1782) from coxiella burnetii (see paper)
43% identity, 99% coverage: 3:394/396 of query aligns to 2:384/389 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 (= V321), E317 (= E323), G343 (= G353), D345 (= D355), T346 (= T356)
- binding magnesium ion: D288 (= D294), G314 (= G320), F321 (= F327), S322 (≠ D328), T325 (= T331)
P0A799 Phosphoglycerate kinase; EC 2.7.2.3 from Escherichia coli (strain K12) (see 3 papers)
44% identity, 100% coverage: 1:395/396 of query aligns to 1:382/387 of P0A799
- M1 (= M1) modified: Initiator methionine, Removed
- K84 (≠ L83) modified: N6-acetyllysine
1zmrA Crystal structure of the e. Coli phosphoglycerate kinase (see paper)
45% identity, 97% coverage: 10:395/396 of query aligns to 9:381/386 of 1zmrA
6yjeA Plasmoodium vivax phosphoglycerate kinase bound to nitrofuran inhibitor from peg3350 and ammonium acetate at ph 5.5
43% identity, 98% coverage: 7:396/396 of query aligns to 10:415/416 of 6yjeA
- active site: R39 (= R36), K215 (= K197), G373 (= G354), G396 (= G377)
- 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 (= G219), G238 (= G220), Y241 (≠ N223), L256 (= L237), F291 (≠ V272), M311 (≠ I292), G312 (vs. gap), L313 (= L293), G340 (= G320), V341 (= V321)
P07378 Phosphoglycerate kinase, glycosomal; Phosphoglycerate kinase C; EC 2.7.2.3 from Trypanosoma brucei brucei (see 2 papers)
39% 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)
39% 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 (≠ S196), K219 (= K201), A238 (≠ G220), Y241 (≠ N223), L311 (= L293), P336 (= P318), G338 (= G320), V339 (= V321), E341 (= E323), G393 (≠ A375), G394 (= G376), G395 (= G377)
13pkA Ternary complex of phosphoglycerate kinase from trypanosoma brucei (see paper)
39% 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 (≠ S196), K219 (= K201), L311 (= L293), P336 (= P318), G338 (= G320), V339 (= V321), E341 (= E323), G371 (= G353), D373 (= D355), S374 (≠ T356)
1ltkC Crystal structure of phosphoglycerate kinase from plasmodium falciparum, in the open conformation
41% identity, 98% coverage: 7:396/396 of query aligns to 18:423/424 of 1ltkC
- active site: R47 (= R36), K223 (= K197), G381 (= G354), G404 (= G377)
- binding adenosine monophosphate: G221 (= G195), A222 (≠ S196), K223 (= K197), G245 (= G219), G246 (= G220), G348 (= G320), V349 (= V321), E351 (= E323), D382 (= D355)
O60101 Phosphoglycerate kinase; EC 2.7.2.3 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
42% identity, 98% coverage: 10:396/396 of query aligns to 13:413/414 of O60101
- Y75 (≠ M71) modified: Phosphotyrosine
- S76 (= S72) modified: Phosphoserine
- S143 (≠ E129) modified: Phosphoserine
- S172 (≠ A154) modified: Phosphoserine
- S173 (= S155) modified: Phosphoserine
- S183 (≠ P167) modified: Phosphoserine
- S253 (= S236) modified: Phosphoserine
- S260 (≠ A243) modified: Phosphoserine
- T299 (≠ S282) modified: Phosphothreonine
- S328 (= S310) modified: Phosphoserine
- S351 (= S333) modified: Phosphoserine
- T373 (= T356) modified: Phosphothreonine
- S387 (≠ T370) modified: Phosphoserine
- S390 (= S373) modified: Phosphoserine
- S412 (≠ E395) modified: Phosphoserine
- S413 (= S396) modified: Phosphoserine
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
42% identity, 99% coverage: 5:396/396 of query aligns to 6:406/407 of 4axxA
- active site: R37 (= R36), K206 (= K197), G364 (= G354), G387 (= G377)
- binding adenosine-5'-diphosphate: G204 (= G195), A205 (≠ S196), K210 (= K201), G228 (= G219), G229 (= G220), N327 (= N316), P329 (= P318), G331 (= G320), V332 (= V321), E334 (= E323), G363 (= G353), G364 (= G354), D365 (= D355), T366 (= T356)
- binding beryllium trifluoride ion: K206 (= K197), K210 (= K201), G363 (= G353)
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
42% identity, 99% coverage: 5:396/396 of query aligns to 6:404/405 of 2wzcA
- active site: R37 (= R36), K204 (= K197), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (≠ S196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (= V321), 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)
42% identity, 99% coverage: 5:396/396 of query aligns to 6:404/405 of 2wzbA
- active site: R37 (= R36), K204 (= K197), G362 (= G354), G385 (= G377)
- binding adenosine-5'-diphosphate: G202 (= G195), A203 (≠ S196), K204 (= K197), K208 (= K201), G226 (= G219), G227 (= G220), N325 (= N316), P327 (= P318), G329 (= G320), V330 (= V321), E332 (= E323), G361 (= G353), D363 (= D355), T364 (= T356)
- binding trifluoromagnesate: K204 (= K197), K208 (= K201), G361 (= G353), G384 (= G376), G385 (= G377)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
41% identity, 99% coverage: 5:396/396 of query aligns to 6:407/408 of 2x15A
- active site: R37 (= R36), K207 (= K197), G365 (= G354), G388 (= G377)
- binding adenosine-5'-diphosphate: G205 (= G195), A206 (≠ S196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), P330 (= P318), G332 (= G320), V333 (= V321), E335 (= E323), G364 (= G353), G365 (= G354), D366 (= D355), T367 (= T356)
- binding adenosine-5'-triphosphate: G205 (= G195), A206 (≠ S196), K207 (= K197), K211 (= K201), G229 (= G219), G230 (= G220), N328 (= N316), G332 (= G320), V333 (= V321), 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)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
42% identity, 99% coverage: 5:396/396 of query aligns to 8:416/417 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 (≠ G235), L257 (= L237), F292 (≠ V272), M312 (≠ L291), G313 (≠ I292), L314 (= L293), G341 (= G320), V342 (= V321)
Query Sequence
>CCNA_03359 FitnessBrowser__Caulo:CCNA_03359
MTFRTLDTADLAGKRALVRVDFNVPVDGGKVADDTRLKAALPTIRFLADKGAKVVLLAHF
DRPKGKVVPEMSLAFVAEPLAALLGAPVAFVGDCVGPAAAEVVNGLADGGVALLENVRFH
AGEEKNDAEFAKALAANGDVYVNDAFSAAHRAHASTEGLAKLLPAYPGVSMQRELEALDA
ALGNPKKPVIGIVGGSKVSTKLDLLNNLVAKLDRLAIGGGMANTFLFAQGHDVGGSLCEK
DLADTAREIMEKAKAAGCELLLPVDVVVAKKVAPGVETAVRSLSEVQADDLILDAGPESA
KRLLAAMDQSLTLIWNGPLGVFEVPPFDEATVSAAKHAASLAKSGKIVAVAGGGDTVAAL
NHAGVSADFTFVSTAGGAFLEWMEGKTLPGVAALES
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