SitesBLAST
Comparing Pf1N1B4_2347 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2347 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)
6pnzA The structure of the aspartate transcarbamoylase trimer from staphylococcus aureus complexed with pala at 2.27 resolution.
38% identity, 89% coverage: 18:315/334 of query aligns to 1:288/293 of 6pnzA
- binding n-(phosphonacetyl)-l-aspartic acid: S48 (= S69), T49 (= T70), R50 (= R71), T51 (= T72), S75 (= S96), K78 (= K99), R100 (= R121), H127 (= H151), R160 (= R184), R210 (= R239), Q212 (= Q241), A253 (≠ G280)
3r7fA Crystal structure of cp-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 90% coverage: 18:319/334 of query aligns to 1:289/291 of 3r7fA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding phosphoric acid mono(formamide)ester: S47 (= S69), T48 (= T70), R49 (= R71), T50 (= T72), R99 (= R121), H127 (= H151), Q130 (= Q154), P249 (= P279), A250 (≠ G280)
- binding phosphate ion: S11 (≠ R28), T12 (≠ R29), Q23 (≠ D40), K26 (≠ R48), E140 (≠ R164), R171 (≠ T195), K241 (= K271), H243 (≠ D273), K272 (≠ N302), K272 (≠ N302), K275 (≠ T305)
3r7dA Crystal structure of unliganded aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 90% coverage: 18:319/334 of query aligns to 1:289/291 of 3r7dA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding phosphate ion: S11 (≠ R28), T12 (≠ R29), T73 (≠ S95), S74 (= S96), K77 (= K99), R171 (≠ T195)
3r7lA Crystal structure of pala-bound aspartate transcarbamoylase from bacillus subtilis (see paper)
38% identity, 90% coverage: 18:319/334 of query aligns to 1:289/290 of 3r7lA
- active site: R49 (= R71), T50 (= T72), K77 (= K99), R99 (= R121), H127 (= H151), Q130 (= Q154), L210 (= L238), P249 (= P279), G277 (= G307)
- binding n-(phosphonacetyl)-l-aspartic acid: S47 (= S69), T48 (= T70), R49 (= R71), T50 (= T72), S74 (= S96), K77 (= K99), R99 (= R121), H127 (= H151), R160 (= R184), R211 (= R239), Q213 (= Q241), A250 (≠ G280)
P05654 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Bacillus subtilis (strain 168) (see paper)
38% identity, 90% coverage: 18:319/334 of query aligns to 1:289/304 of P05654
Sites not aligning to the query:
- 303 modified: Phosphoserine
4bjhB Crystal structure of the aquifex reactor complex formed by dihydroorotase (h180a, h232a) with dihydroorotate and aspartate transcarbamoylase with n-(phosphonacetyl)-l-aspartate (pala) (see paper)
38% identity, 91% coverage: 18:320/334 of query aligns to 1:291/291 of 4bjhB
- active site: R47 (= R71), T48 (= T72), K75 (= K99), R97 (= R121), H126 (= H151), Q129 (= Q154)
- binding n-(phosphonacetyl)-l-aspartic acid: S45 (= S69), T46 (= T70), R47 (= R71), T48 (= T72), R97 (= R121), H126 (= H151), R159 (= R184), V160 (= V185), R213 (= R239), Q215 (= Q241), G251 (= G280)
3d6nB Crystal structure of aquifex dihydroorotase activated by aspartate transcarbamoylase (see paper)
38% identity, 91% coverage: 18:320/334 of query aligns to 1:291/291 of 3d6nB
- active site: R47 (= R71), T48 (= T72), K75 (= K99), R97 (= R121), H126 (= H151), Q129 (= Q154)
- binding citrate anion: T48 (= T72), R97 (= R121), H126 (= H151), R159 (= R184), V160 (= V185), R213 (= R239), G251 (= G280)
8bplA Aspartate transcarbamoylase mutant (n2045c, r2238c) from chaetomium thermophilum cad-like bound to carbamoyl phosphate (see paper)
36% identity, 90% coverage: 20:320/334 of query aligns to 17:316/316 of 8bplA
4eknB Structure of the catalytic chain of methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form (see paper)
36% identity, 90% coverage: 18:316/334 of query aligns to 1:297/304 of 4eknB
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2hseA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding aspartic acid: R54 (= R71), T55 (= T72), S58 (≠ T75), R105 (= R121), H134 (= H151), Q137 (= Q154), R167 (= R184), R229 (= R239), Q231 (= Q241), L267 (≠ G280), P268 (= P281), A289 (≠ V304), R296 (= R311)
- binding phosphonoacetamide: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), L267 (≠ G280)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2a0fA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding phosphonoacetamide: R54 (= R71), T55 (= T72), H134 (= H151), Q137 (= Q154), L267 (≠ G280)
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2ipoA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), T168 (≠ V185), R229 (= R239), L267 (≠ G280)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2h3eA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S69), T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), R229 (= R239), L267 (≠ G280)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2fzkA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T72), H134 (= H151), Q137 (= Q154), T168 (≠ V185), R229 (= R239), P266 (= P279), L267 (≠ G280), R296 (= R311)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2fzgA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S69), R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151), R167 (= R184), T168 (≠ V185), R229 (= R239), P266 (= P279), L267 (≠ G280)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2fzcA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S69), R54 (= R71), T55 (= T72), R105 (= R121), R167 (= R184), T168 (≠ V185), P266 (= P279), L267 (≠ G280)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 2airA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S69), T53 (= T70), R54 (= R71), R105 (= R121)
- binding phosphoric acid mono(formamide)ester: R54 (= R71), T55 (= T72), R105 (= R121), H134 (= H151)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 1za2A
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding phosphoric acid mono(formamide)ester: T53 (= T70), R54 (= R71), T55 (= T72), R105 (= R121), R167 (= R184), T168 (≠ V185), L267 (≠ G280)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 1r0cA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding n-carbamoyl-l-aspartate: S52 (= S69), R54 (= R71), R105 (= R121)
- binding phosphate ion: R105 (= R121), H134 (= H151), Q137 (= Q154)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
35% identity, 90% coverage: 19:320/334 of query aligns to 7:305/310 of 1r0bA
- active site: R54 (= R71), T55 (= T72), K84 (= K99), R105 (= R121), H134 (= H151), Q137 (= Q154), T228 (≠ L238), P266 (= P279), G292 (= G307)
- binding citrate anion: H134 (= H151), R167 (= R184), R229 (= R239), Q231 (= Q241), P266 (= P279), P268 (= P281)
- binding phosphate ion: S80 (= S95), K84 (= K99)
Query Sequence
>Pf1N1B4_2347 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_2347
MTPLETKRPLQLNDQGQLRHFLSLDGLRRELLTEILDTADSFLEVGARAVKKVPLLRGKT
VCNVFFENSTRTRTTFELAAQRLSADVITLNVSTSSASKGETLLDTLRNLEAMAADMFVV
RHGDSGAAHFIAEHVCPQVAIINGGDGRHAHPTQGMLDMLTIRRHKGGFENLSVAIVGDI
LHSRVARSNMLALKTLGCPDIRVIAPKTLLPIGIEQYGVKVYTDMTEGLKDVDVVIMLRL
QRERMTGGLLPSEGEFYRLFGLTTARLAGAKPDCIVMHPGPINRGVEIESAVADGPHSVI
LNQVTYGIAIRMAVLSMAMSGQTAQRQFEQENAQ
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