SitesBLAST
Comparing CA265_RS01880 FitnessBrowser__Pedo557:CA265_RS01880 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)
P40924 Phosphoglycerate kinase; EC 2.7.2.3 from Bacillus subtilis (strain 168) (see paper)
55% identity, 99% coverage: 3:396/397 of query aligns to 5:392/394 of P40924
- S183 (≠ N184) modified: Phosphoserine
- T299 (≠ S300) modified: Phosphothreonine
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)
53% identity, 99% coverage: 3:395/397 of query aligns to 5:394/654 of P36204
- R36 (= R35) binding
- R118 (= R117) binding
- R151 (= R150) binding
1vpeA Crystallographic analysis of phosphoglycerate kinase from the hyperthermophilic bacterium thermotoga maritima (see paper)
52% identity, 99% coverage: 3:396/397 of query aligns to 4:394/398 of 1vpeA
- active site: R35 (= R35), K196 (= K198), G353 (= G355), G376 (= G378)
- binding phosphoaminophosphonic acid-adenylate ester: G194 (= G196), A195 (= A197), K196 (= K198), K200 (= K202), G218 (= G220), A219 (≠ G221), N316 (= N317), P318 (= P319), G320 (= G321), V321 (= V322), E323 (= E324), G352 (= G354), G353 (= G355), D354 (= D356), S355 (= S357)
1phpA Structure of the adp complex of the 3-phosphoglycerate kinase from bacillus stearothermophilus at 1.65 angstroms (see paper)
55% identity, 99% coverage: 3:395/397 of query aligns to 5:391/394 of 1phpA
- active site: R36 (= R35), K197 (= K198), G351 (= G355), G374 (= G378)
- binding adenosine-5'-diphosphate: G195 (= G196), K201 (= K202), G219 (= G220), G220 (= G221), L237 (= L238), N316 (= N317), P318 (= P319), G320 (= G321), V321 (= V322), E323 (= E324), G350 (= G354), D352 (= D356), S353 (= S357)
P18912 Phosphoglycerate kinase; EC 2.7.2.3 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
55% identity, 99% coverage: 3:395/397 of query aligns to 5:391/394 of P18912
2wzcA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and aluminium tetrafluoride (see paper)
51% identity, 99% coverage: 3:396/397 of query aligns to 6:403/405 of 2wzcA
- active site: R37 (= R35), K204 (= K198), G362 (= G355), G385 (= G378)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (= A197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (= V322), E332 (= E324), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding tetrafluoroaluminate ion: R37 (= R35), K204 (= K198), K208 (= K202), G361 (= G354), G362 (= G355), G384 (= G377)
2wzbA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp, 3pg and magnesium trifluoride (see paper)
51% identity, 99% coverage: 3:396/397 of query aligns to 6:403/405 of 2wzbA
- active site: R37 (= R35), K204 (= K198), G362 (= G355), G385 (= G378)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (= A197), K204 (= K198), K208 (= K202), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (= V322), E332 (= E324), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding trifluoromagnesate: K204 (= K198), K208 (= K202), G361 (= G354), G384 (= G377), G385 (= G378)
2wzdA The catalytically active fully closed conformation of human phosphoglycerate kinase k219a mutant in complex with adp, 3pg and aluminium trifluoride (see paper)
50% identity, 99% coverage: 3:396/397 of query aligns to 6:403/405 of 2wzdA
- active site: R37 (= R35), K204 (= K198), G362 (= G355), G385 (= G378)
- binding adenosine-5'-diphosphate: G202 (= G196), A203 (= A197), K204 (= K198), G226 (= G220), G227 (= G221), N325 (= N317), P327 (= P319), G329 (= G321), V330 (= V322), E332 (= E324), G361 (= G354), D363 (= D356), T364 (≠ S357)
- binding aluminum fluoride: R37 (= R35), K204 (= K198), G361 (= G354), G362 (= G355), G384 (= G377)
2x15A The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp and 1,3- bisphosphoglycerate
50% identity, 99% coverage: 3:396/397 of query aligns to 6:406/408 of 2x15A
- active site: R37 (= R35), K207 (= K198), G365 (= G355), G388 (= G378)
- binding adenosine-5'-diphosphate: G205 (= G196), A206 (= A197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), P330 (= P319), G332 (= G321), V333 (= V322), E335 (= E324), G364 (= G354), G365 (= G355), D366 (= D356), T367 (≠ S357)
- binding adenosine-5'-triphosphate: G205 (= G196), A206 (= A197), K207 (= K198), K211 (= K202), G229 (= G220), G230 (= G221), N328 (= N317), G332 (= G321), V333 (= V322), E335 (= E324), G364 (= G354), G365 (= G355), D366 (= D356), T367 (≠ S357), G387 (= G377), G388 (= G378)
- binding 1,3-bisphosphoglyceric acid: D22 (= D19), N24 (= N21), R37 (= R35), H61 (= H58), R64 (= R61), R121 (= R117), R162 (= R150), K207 (= K198), K211 (= K202), G364 (= G354), G387 (= G377), G388 (= G378)
1vjcA Structure of pig muscle pgk complexed with mgatp (see paper)
50% identity, 99% coverage: 3:396/397 of query aligns to 7:414/416 of 1vjcA
4axxA The catalytically active fully closed conformation of human phosphoglycerate kinase in complex with adp 3-phosphoglycerate and beryllium trifluoride
50% identity, 99% coverage: 3:396/397 of query aligns to 6:405/407 of 4axxA
- active site: R37 (= R35), K206 (= K198), G364 (= G355), G387 (= G378)
- binding adenosine-5'-diphosphate: G204 (= G196), A205 (= A197), K210 (= K202), G228 (= G220), G229 (= G221), N327 (= N317), P329 (= P319), G331 (= G321), V332 (= V322), E334 (= E324), G363 (= G354), G364 (= G355), D365 (= D356), T366 (≠ S357)
- binding beryllium trifluoride ion: K206 (= K198), K210 (= K202), G363 (= G354)
1kf0A Crystal structure of pig muscle phosphoglycerate kinase ternary complex with amp-pcp and 3pg (see paper)
50% identity, 99% coverage: 3:396/397 of query aligns to 7:414/416 of 1kf0A
Q7SIB7 Phosphoglycerate kinase 1; EC 2.7.2.3 from Sus scrofa (Pig) (see 2 papers)
50% identity, 99% coverage: 3:396/397 of query aligns to 8:415/417 of Q7SIB7
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)
49% identity, 99% coverage: 3:396/397 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 (= L82) to P: in PGK1D; with congenital non-spherocytic anemia; variant Matsue; dbSNP:rs137852531
- K97 (≠ D91) modified: N6-(2-hydroxyisobutyryl)lysine; alternate
- R123 (= R117) binding
- K131 (= K124) modified: N6-malonyllysine; alternate
- G158 (= G137) to V: in PGK1D; with chronic hemolytic anemia; variant Shizuoka; dbSNP:rs137852532
- D164 (= D143) to V: in PGK1D; with chronic hemolytic anemia and intellectual disability; variant Amiens; dbSNP:rs137852538
- R171 (= R150) binding
- K191 (≠ A173) natural variant: Missing (in PGK1D; with chronic hemolytic anemia; variant Alabama)
- R206 (= R188) to P: in PGK1D; with chronic hemolytic anemia; variant Uppsala; dbSNP:rs137852529
- K216 (= K198) modified: N6-(2-hydroxyisobutyryl)lysine
- K220 (= K202) binding ; modified: N6-(2-hydroxyisobutyryl)lysine
- E252 (= E233) to A: in PGK1D; with chronic hemolytic anemia; variant Antwerp
- V266 (≠ S247) to M: in PGK1D; with chronic non-spherocytic hemolytic anemia; variant Tokyo; dbSNP:rs431905501
- D268 (≠ E249) to N: in Munchen; 21% of activity; dbSNP:rs137852528
- D285 (= D266) to V: in PGK1D; with chronic hemolytic anemia; variant Herlev; 50% of activity; dbSNP:rs137852535
- G313 (= G293) binding
- D315 (= D295) to N: in PGK1D; with rhabdomyolysis; variant Creteil
- C316 (≠ I296) to R: in PGK1D; with chronic hemolytic anemia; variant Michigan; dbSNP:rs137852533
- K323 (≠ L303) modified: N6-(2-hydroxyisobutyryl)lysine
- E344 (= E324) binding
- T352 (= T332) to N: in dbSNP:rs137852530
- GGDT 373:376 (≠ GGDS 354:357) 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)
49% identity, 99% coverage: 3:396/397 of query aligns to 6:413/414 of 2y3iA
- active site: R37 (= R35), K214 (= K198), G372 (= G355), G395 (= G378)
- binding tetrafluoroaluminate ion: K214 (= K198), G371 (= G354), G372 (= G355), G394 (= G377)
- binding l-adenosine-5'-diphosphate: G212 (= G196), A213 (= A197), F290 (= F273), N335 (= N317), G339 (= G321), V340 (= V322), E342 (= E324), G371 (= G354), G372 (= G355), D373 (= D356), T374 (≠ S357)
4o33A Crystal structure of human pgk1 3pg and terazosin(tzn) ternary complex (see paper)
49% identity, 99% coverage: 3:396/397 of query aligns to 8:415/417 of 4o33A
- active site: R39 (= R35), K216 (= K198), G374 (= G355), G397 (= G378)
- binding [4-(4-amino-6,7-dimethoxyquinazolin-2-yl)piperazin-1-yl][(2R)-tetrahydrofuran-2-yl]methanone: G238 (= G220), G239 (= G221), T255 (= T236), L257 (= L238), F292 (= F273), M312 (= M292), G313 (= G293), L314 (= L294), G341 (= G321), V342 (= V322)
P09041 Phosphoglycerate kinase 2; Phosphoglycerate kinase, testis specific; EC 2.7.2.3 from Mus musculus (Mouse) (see paper)
49% identity, 99% coverage: 3:396/397 of query aligns to 8:415/417 of P09041
2paaA Crystal structure of phosphoglycerate kinase-2 bound to atp and 3pg (see paper)
48% identity, 99% coverage: 3:396/397 of query aligns to 4:411/413 of 2paaA
- active site: R35 (= R35), K212 (= K198), G370 (= G355), G393 (= G378)
- binding adenosine-5'-triphosphate: G210 (= G196), A211 (= A197), K216 (= K202), G235 (= G221), L253 (= L238), G309 (= G293), L310 (= L294), G334 (= G318), G337 (= G321), V338 (= V322), E340 (= E324), D371 (= D356)
5m1rA X-ray structure of human g166d pgk-1 mutant (see paper)
49% identity, 99% coverage: 3:396/397 of query aligns to 7:414/416 of 5m1rA
- active site: R38 (= R35), K215 (= K198), G373 (= G355), G396 (= G378)
- binding adenosine-5'-diphosphate: G213 (= G196), A214 (= A197), K219 (= K202), G237 (= G220), G238 (= G221), L256 (= L238), G340 (= G321), V341 (= V322), E343 (= E324), D374 (= D356), T375 (≠ S357)
- binding magnesium ion: R150 (≠ A130), A151 (≠ E131), G372 (= G354), T375 (≠ S357)
P00560 Phosphoglycerate kinase; EC 2.7.2.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
50% identity, 98% coverage: 3:392/397 of query aligns to 8:409/416 of P00560
- R22 (= R17) mutation to K: 2-fold reduction of Vmax.; mutation to M: 7-fold reduction of Vmax.
- R39 (= R35) binding
- R122 (= R117) binding
- R169 (= R150) binding
Query Sequence
>CA265_RS01880 FitnessBrowser__Pedo557:CA265_RS01880
MNTIDQFDFKDKKALIRVDFNVPLDDEFKITDDKRIRAALPTISKILKDGGAVILMSHLG
RPKDGPTDKYSLKHILSDLSALVGVEVKFADDCIGESAVKQAADLKSGEVLLLENLRFYK
EEEKGDVAFAEKLSKLGDVYVNDAFGTAHRAHASTSIIAQFFPDAKYFGYLMASEVENAE
KILNHAERPFTAIMGGAKVSDKILLIEKLLDKVDNLIIGGGMAYTFAKAQGGEIGTSLLE
ADKQELSLELIEKAKAKGVNLILPVDTVIADKFANDADKKDVTSGQIPADWMGLDIGPKS
VALFQDVIKNSKTLLWNGPMGVFEMESFQVGTKAVAEAVVAATKDNGAFSLIGGGDSAAA
IAKFGMEDEVSYVSTGGGALLEYMEGKELPGVKAING
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