SitesBLAST
Comparing BWI76_RS02995 FitnessBrowser__Koxy:BWI76_RS02995 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)
P0A786 Aspartate carbamoyltransferase catalytic subunit; Aspartate transcarbamylase; ATCase; EC 2.1.3.2 from Escherichia coli (strain K12) (see 4 papers)
93% identity, 100% coverage: 1:311/311 of query aligns to 1:311/311 of P0A786
- M1 (= M1) modified: Initiator methionine, Removed
- R55 (= R55) binding carbamoyl phosphate
- T56 (= T56) binding carbamoyl phosphate
- R106 (= R106) binding carbamoyl phosphate
- H135 (= H135) binding carbamoyl phosphate
- Q138 (= Q138) binding carbamoyl phosphate
- L268 (= L268) binding carbamoyl phosphate
- P269 (= P269) binding carbamoyl phosphate
2ipoA E. Coli aspartate transcarbamoylase complexed with n-phosphonacetyl-l- asparagine (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2ipoA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding n~2~-(phosphonoacetyl)-l-asparagine: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R230), L267 (= L268)
2h3eA Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of n-phosphonacetyl-l-isoasparagine at 2.3a resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2h3eA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding (s)-4-amino-4-oxo-3-(2-phosphonoacetamido)butanoic acid: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), R229 (= R230), L267 (= L268)
2fzkA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.50 resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzkA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding 3,5-bis[(phosphonoacetyl)amino]benzoic acid: T55 (= T56), H134 (= H135), Q137 (= Q138), T168 (= T169), R229 (= R230), P266 (= P267), L267 (= L268), R296 (= R297)
2fzgA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.25 resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzgA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding {1,3-phenylenebis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135), R167 (= R168), T168 (= T169), R229 (= R230), P266 (= P267), L267 (= L268)
2fzcA The structure of wild-type e. Coli aspartate transcarbamoylase in complex with novel t state inhibitors at 2.10 resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2fzcA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding {ethane-1,2-diylbis[imino(2-oxoethane-2,1-diyl)]}bis(phosphonic acid): S52 (= S53), R54 (= R55), T55 (= T56), R105 (= R106), R167 (= R168), T168 (= T169), P266 (= P267), L267 (= L268)
2airA T-state active site of aspartate transcarbamylase:crystal structure of the carbamyl phosphate and l-alanosine ligated enzyme (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2airA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding 3-[hydroxy(nitroso)amino]-l-alanine: S52 (= S53), T53 (= T54), R54 (= R55), R105 (= R106)
- binding phosphoric acid mono(formamide)ester: R54 (= R55), T55 (= T56), R105 (= R106), H134 (= H135)
1za2A Structure of wild-type e. Coli aspartate transcarbamoylase in the presence of ctp, carbamoyl phosphate at 2.50 a resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1za2A
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding phosphoric acid mono(formamide)ester: T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), R167 (= R168), T168 (= T169), L267 (= L268)
1r0cA Products in the t state of aspartate transcarbamylase: crystal structure of the phosphate and n-carbamyl-l-aspartate ligated enzyme (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1r0cA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding n-carbamoyl-l-aspartate: S52 (= S53), R54 (= R55), R105 (= R106)
- binding phosphate ion: R105 (= R106), H134 (= H135), Q137 (= Q138)
1r0bA Aspartate transcarbamylase (atcase) of escherichia coli: a new crystalline r state bound to pala, or to product analogues phosphate and citrate (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 1r0bA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding citrate anion: H134 (= H135), R167 (= R168), R229 (= R230), Q231 (= Q232), P266 (= P267), P268 (= P269)
- binding phosphate ion: S80 (= S81), K84 (= K85)
2hseA Structure of d236a e. Coli aspartate transcarbamoylase in the presence of phosphonoacetamide and l-aspartate at 2.60 a resolution
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2hseA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding aspartic acid: R54 (= R55), T55 (= T56), S58 (= S59), R105 (= R106), H134 (= H135), Q137 (= Q138), R167 (= R168), R229 (= R230), Q231 (= Q232), L267 (= L268), P268 (= P269), A289 (= A290), R296 (= R297)
- binding phosphonoacetamide: S52 (= S53), T53 (= T54), R54 (= R55), T55 (= T56), R105 (= R106), L267 (= L268)
2a0fA Structure of d236a mutant e. Coli aspartate transcarbamoylase in presence of phosphonoacetamide at 2.90 a resolution (see paper)
93% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2a0fA
- active site: R54 (= R55), T55 (= T56), K84 (= K85), R105 (= R106), H134 (= H135), Q137 (= Q138), T228 (= T229), P266 (= P267), G292 (= G293)
- binding phosphonoacetamide: R54 (= R55), T55 (= T56), H134 (= H135), Q137 (= Q138), L267 (= L268)
5vmqC Structure of the r105a mutant catalytic trimer of escherichia coli aspartate transcarbamoylase at 2.0-a resolution (see paper)
93% identity, 99% coverage: 2:309/311 of query aligns to 1:308/309 of 5vmqC
2at1A Crystal structures of phosphonoacetamide ligated t and phosphonoacetamide and malonate ligated r states of aspartate carbamoyltransferase at 2.8-angstroms resolution and neutral ph (see paper)
92% identity, 100% coverage: 2:311/311 of query aligns to 1:310/310 of 2at1A