SitesBLAST
Comparing AZOBR_RS33555 FitnessBrowser__azobra:AZOBR_RS33555 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)
7k3pA The structure of the udp-glc/glcnac 4-epimerase from the human pathogen campylobacter jejuni
46% identity, 97% coverage: 10:330/332 of query aligns to 3:328/329 of 7k3pA
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), Y12 (= Y19), I13 (= I20), D32 (= D39), N33 (= N40), S35 (= S42), G37 (= G44), D57 (= D59), L58 (≠ V60), F79 (= F81), A80 (= A82), I83 (= I85), N98 (= N100), Y147 (= Y149), K151 (= K153), Y175 (= Y176), N177 (= N178), V178 (= V179)
2c20A Crystal structure of udp-glucose 4-epimerase
45% identity, 96% coverage: 11:330/332 of query aligns to 3:322/329 of 2c20A
- active site: T117 (= T125), A118 (= A126), A119 (= A127), Y141 (= Y149), K145 (= K153), H184 (≠ T192)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), Q34 (≠ S42), T35 (= T43), G36 (= G44), D51 (= D59), L52 (≠ V60), F73 (= F81), A74 (= A82), A75 (≠ G83), N92 (= N100), Y141 (= Y149), K145 (= K153), Y168 (= Y176), F169 (= F177), V171 (= V179), H184 (≠ T192)
- binding zinc ion: E182 (≠ Q190), H184 (≠ T192), E187 (≠ A195), H189 (= H197)
4twrA Structure of udp-glucose 4-epimerase from brucella abortus
48% identity, 95% coverage: 9:324/332 of query aligns to 2:316/325 of 4twrA
- active site: S117 (≠ T125), C118 (≠ A126), A119 (= A127), Y141 (= Y149), K145 (= K153), H184 (≠ T192), H189 (= H197)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), F12 (≠ Y19), I13 (= I20), D32 (= D39), N33 (= N40), L34 (= L41), S35 (= S42), T36 (= T43), G37 (= G44), D51 (= D59), I52 (≠ V60), F73 (= F81), A74 (= A82), A75 (≠ G83), N92 (= N100), S115 (= S123), K145 (= K153), Y168 (= Y176), A171 (≠ V179), H184 (≠ T192)
- binding zinc ion: E182 (≠ Q190), H184 (≠ T192), E187 (≠ A195), H189 (= H197)
Q9SA77 UDP-arabinose 4-epimerase 1; UDP-D-xylose 4-epimerase 1; EC 5.1.3.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
41% identity, 96% coverage: 11:329/332 of query aligns to 73:403/419 of Q9SA77
- G275 (≠ V201) mutation to D: In mur4-1; 50% reduction in L-Ara in cell wall material.
- R304 (= R229) mutation to Q: In mur4-3; 50% reduction in L-Ara in cell wall material.
1ek6A Structure of human udp-galactose 4-epimerase complexed with nadh and udp-glucose (see paper)
42% identity, 97% coverage: 9:330/332 of query aligns to 3:339/346 of 1ek6A
- active site: S132 (≠ T125), A133 (= A126), T134 (≠ A127), Y157 (= Y149), K161 (= K153)
- binding 1,4-dihydronicotinamide adenine dinucleotide: G9 (= G15), G12 (= G18), Y13 (= Y19), I14 (= I20), D33 (= D39), N34 (= N40), H36 (≠ S42), N37 (≠ T43), D66 (= D59), I67 (≠ V60), F88 (= F81), A89 (= A82), G90 (= G83), K92 (≠ I85), S130 (= S123), S131 (= S124), S132 (≠ T125), Y157 (= Y149), K161 (= K153), Y185 (= Y176), P188 (≠ V179)
- binding uridine-5'-diphosphate-glucose: S132 (≠ T125), Y157 (= Y149), F186 (= F177), N187 (= N178), N207 (≠ H197), L208 (= L198), N224 (≠ S214), V225 (≠ I215), F226 (= F216), R239 (= R229), Y241 (= Y231), V277 (= V267), R300 (= R290), D303 (= D293)
Q14376 UDP-glucose 4-epimerase; Galactowaldenase; UDP-N-acetylgalactosamine 4-epimerase; UDP-GalNAc 4-epimerase; UDP-N-acetylglucosamine 4-epimerase; UDP-GlcNAc 4-epimerase; UDP-galactose 4-epimerase; EC 5.1.3.2; EC 5.1.3.7 from Homo sapiens (Human) (see 13 papers)
42% identity, 97% coverage: 9:330/332 of query aligns to 3:339/348 of Q14376
- GYI 12:14 (= GYI 18:20) binding
- DNFHN 33:37 (≠ DNLST 39:43) binding
- N34 (= N40) to S: in GALAC3; peripheral; nearly normal activity towards UDP-galactose; dbSNP:rs121908046
- DI 66:67 (≠ DV 59:60) binding
- F88 (= F81) binding
- G90 (= G83) to E: in GALAC3; 800-fold decrease in UDP-galactose epimerization activity; dbSNP:rs28940882
- K92 (≠ I85) binding
- V94 (= V87) to M: in GALAC3; generalized; 30-fold decrease in UDP-galactose epimerization activity; 2-fold decrease in affinity for UDP-galactose; 24% of normal activity with respect to UDP-N-acetylgalactosamine; dbSNP:rs121908047
- D103 (≠ A96) to G: in GALAC3; 7-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine; dbSNP:rs28940883
- S132 (≠ T125) mutation to A: Loss of activity.
- SAT 132:134 (≠ TAA 125:127) binding
- Y157 (= Y149) active site, Proton acceptor; mutation to F: Loss of activity.
- K161 (= K153) binding
- A180 (≠ S171) to V: in dbSNP:rs3204468
- L183 (= L174) to P: in GALAC3; peripheral; 3-fold decrease in UDP-galactose epimerization activity; dbSNP:rs121908045
- Y185 (= Y176) binding
- YFN 185:187 (= YFN 176:178) binding
- N--NL 206:208 (≠ TATHL 194:198) binding
- NVF 224:226 (≠ SIF 214:216) binding
- R239 (= R229) binding
- K257 (≠ H247) to R: in GALAC3; 7-fold decrease in UDP-galactose epimerization activity; does not affect affinity for UDP-galactose; dbSNP:rs28940884
- REGD 300:303 (≠ RPGD 290:293) binding
- C307 (≠ L297) mutation to Y: No effect on activity towards UDP-galactose. Loss of activity towards UDP-N-acetylgalactosamine.
- L313 (≠ R303) to M: in GALAC3; 6-fold decrease in UDP-galactose epimerization activity; very mild decrease in activity towards UDP-N-acetylgalactosamine; dbSNP:rs3180383
- G319 (= G309) to E: in GALAC3; nearly normal activity towards UDP-galactose; mild impairment under conditions of substrate limitation; dbSNP:rs28940885
- R335 (≠ A326) to H: in GALAC3; 2-fold decrease in UDP-galactose epimerization activity; dbSNP:rs368637540
1hzjA Human udp-galactose 4-epimerase: accommodation of udp-n- acetylglucosamine within the active site (see paper)
42% identity, 97% coverage: 9:330/332 of query aligns to 2:338/345 of 1hzjA
- active site: S131 (≠ T125), A132 (= A126), T133 (≠ A127), Y156 (= Y149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), Y12 (= Y19), I13 (= I20), D32 (= D39), N33 (= N40), H35 (≠ S42), N36 (≠ T43), D65 (= D59), I66 (≠ V60), F87 (= F81), A88 (= A82), G89 (= G83), K91 (≠ I85), S129 (= S123), S131 (≠ T125), Y156 (= Y149), K160 (= K153), Y184 (= Y176), P187 (≠ V179)
- binding uridine-diphosphate-n-acetylglucosamine: N186 (= N178), N206 (≠ H197), L207 (= L198), N223 (≠ S214), V224 (≠ I215), F225 (= F216), R238 (= R229), Y240 (= Y231), V276 (= V267), R299 (= R290), D302 (= D293)
1i3lA Molecular basis for severe epimerase-deficiency galactosemia: x-ray structure of the human v94m-substituted udp-galactose 4-epimerase (see paper)
41% identity, 97% coverage: 9:330/332 of query aligns to 2:338/347 of 1i3lA
- active site: S131 (≠ T125), A132 (= A126), T133 (≠ A127), Y156 (= Y149), K160 (= K153)
- binding galactose-uridine-5'-diphosphate: N186 (= N178), N206 (≠ H197), L207 (= L198), N223 (≠ S214), V224 (≠ I215), F225 (= F216), R238 (= R229), Y240 (= Y231), V276 (= V267), R299 (= R290), D302 (= D293)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), Y12 (= Y19), I13 (= I20), D32 (= D39), N33 (= N40), H35 (≠ S42), N36 (≠ T43), D65 (= D59), I66 (≠ V60), F87 (= F81), A88 (= A82), G89 (= G83), K91 (≠ I85), S129 (= S123), S130 (= S124), S131 (≠ T125), Y156 (= Y149), K160 (= K153), Y184 (= Y176), P187 (≠ V179)
1i3kA Molecular basis for severe epimerase-deficiency galactosemia: x-ray structure of the human v94m-substituted udp-galactose 4-epimerase (see paper)
41% identity, 97% coverage: 9:330/332 of query aligns to 2:338/347 of 1i3kA
- active site: S131 (≠ T125), A132 (= A126), T133 (≠ A127), Y156 (= Y149), K160 (= K153)
- binding nicotinamide-adenine-dinucleotide: G8 (= G15), G11 (= G18), Y12 (= Y19), I13 (= I20), D32 (= D39), N33 (= N40), H35 (≠ S42), N36 (≠ T43), D65 (= D59), I66 (≠ V60), F87 (= F81), A88 (= A82), G89 (= G83), K91 (≠ I85), S129 (= S123), S131 (≠ T125), Y156 (= Y149), K160 (= K153), Y184 (= Y176), P187 (≠ V179)
- binding uridine-5'-diphosphate-glucose: F185 (= F177), N186 (= N178), N206 (≠ H197), L207 (= L198), N223 (≠ S214), V224 (≠ I215), F225 (= F216), R238 (= R229), Y240 (= Y231), V276 (= V267), R299 (= R290), D302 (= D293)
2udpA Udp-galactose 4-epimerase complexed with udp-phenol (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 2udpA
- active site: S124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), L33 (= L41), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), S122 (= S123), S124 (≠ T125), Y149 (= Y149), K153 (= K153), Y177 (= Y176)
- binding phenyl-uridine-5'-diphosphate: N179 (= N178), N199 (≠ H197), L200 (= L198), A216 (≠ S214), I217 (= I215), F218 (= F216), R231 (= R229), Y233 (= Y231), V269 (= V267), R292 (= R290), D295 (= D293)
1udcA Structure of udp-galactose-4-epimerase complexed with udp-mannose (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1udcA
- active site: S124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), S122 (= S123), Y149 (= Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding uridine-5'-diphosphate-mannose: T126 (≠ A127), Y149 (= Y149), N179 (= N178), N199 (≠ H197), L200 (= L198), L215 (= L213), A216 (≠ S214), I217 (= I215), F218 (= F216), R231 (= R229), Y233 (= Y231), V269 (= V267), R292 (= R290)
P09147 UDP-glucose 4-epimerase; Galactowaldenase; UDP-galactose 4-epimerase; EC 5.1.3.2 from Escherichia coli (strain K12) (see 10 papers)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of P09147
- YI 11:12 (= YI 19:20) binding
- DNLCNS 31:36 (≠ DNLSTG 39:44) binding
- DI 58:59 (≠ DV 59:60) binding
- FAGLK 80:84 (≠ FAGSI 81:85) binding
- N99 (= N100) binding
- S124 (≠ T125) binding ; mutation to A: No major structural changes. Catalytic efficiency is very low and affinity binding is 21% of the wild-type enzyme.; mutation to T: No major structural changes. Catalytic efficiency is about 30% of that of the wild-type enzyme, and affinity binding is similar to that of the native enzyme.
- Y149 (= Y149) active site, Proton acceptor; binding ; mutation to F: No major structural changes. Catalytic efficiency is very low and affinity binding is 12% of the wild-type enzyme.
- K153 (= K153) binding ; mutation to A: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH.; mutation to M: Decreases the catalytic activity. Not reduced by sugars in the presence or absence of UMP. It contains very little NADH.
- F178 (= F177) binding
- Y299 (≠ L297) mutation to C: Loss of epimerase activity with UDP-Gal by almost 5-fold, but it results in a gain of epimerase activity with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) by 230-fold with minimal changes in its three-dimensional structure.
1udaA Structure of udp-galactose-4-epimerase complexed with udp-4-deoxy-4- fluoro-alpha-d-galactose (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1udaA
- active site: S124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), L33 (= L41), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), S122 (= S123), Y149 (= Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding uridine-5'-diphosphate-4-deoxy-4-fluoro-alpha-d-galactose: T126 (≠ A127), N179 (= N178), N199 (≠ H197), L200 (= L198), A216 (≠ S214), I217 (= I215), F218 (= F216), R231 (= R229), Y233 (= Y231), R292 (= R290), D295 (= D293), Y299 (≠ L297)
1naiA Udp-galactose 4-epimerase from escherichia coli, oxidized (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1naiA
- active site: S124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), L33 (= L41), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), Y149 (= Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding 1,3-propandiol: N35 (≠ T43), K84 (≠ I85), E191 (vs. gap), P193 (vs. gap)
- binding uridine-5'-diphosphate: N179 (= N178), N199 (≠ H197), L200 (= L198), L215 (= L213), A216 (≠ S214), R231 (= R229), Y233 (= Y231), R292 (= R290)
1lrjA Crystal structure of e. Coli udp-galactose 4-epimerase complexed with udp-n-acetylglucosamine (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1lrjA
- active site: S124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), L33 (= L41), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), Y149 (= Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding uridine-diphosphate-n-acetylglucosamine: V86 (= V87), S124 (≠ T125), F178 (= F177), N179 (= N178), L200 (= L198), L215 (= L213), A216 (≠ S214), F218 (= F216), R231 (= R229), Y233 (= Y231), V269 (= V267), R292 (= R290), D295 (= D293)
1kvrA Udp-galactose 4-epimerase complexed with udp-phenol (see paper)
43% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1kvrA
- active site: A124 (≠ T125), A125 (= A126), T126 (≠ A127), Y149 (= Y149), K153 (= K153), M189 (≠ T188)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), S122 (= S123), S123 (= S124), Y149 (= Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding uridine-5'-diphosphate: N179 (= N178), N198 (≠ T194), N199 (≠ H197), L200 (= L198), A216 (≠ S214), I217 (= I215), F218 (= F216), R231 (= R229), Y233 (= Y231), V269 (= V267), R292 (= R290), D295 (= D293)
1a9yA Udp-galactose 4-epimerase mutant s124a/y149f complexed with udp- glucose (see paper)
42% identity, 96% coverage: 10:328/332 of query aligns to 2:329/338 of 1a9yA
- active site: A124 (≠ T125), A125 (= A126), T126 (≠ A127), F149 (≠ Y149), K153 (= K153)
- binding nicotinamide-adenine-dinucleotide: G7 (= G15), G10 (= G18), Y11 (= Y19), I12 (= I20), D31 (= D39), N32 (= N40), C34 (≠ S42), N35 (≠ T43), S36 (≠ G44), D58 (= D59), I59 (≠ V60), F80 (= F81), A81 (= A82), G82 (= G83), K84 (≠ I85), S122 (= S123), S123 (= S124), F149 (≠ Y149), K153 (= K153), Y177 (= Y176), P180 (≠ V179)
- binding uridine-5'-diphosphate-glucose: A125 (= A126), T126 (≠ A127), N179 (= N178), N199 (≠ H197), L200 (= L198), A216 (≠ S214), I217 (= I215), F218 (= F216), R231 (= R229), Y233 (= Y231), R292 (= R290), D295 (= D293), Y299 (≠ L297)
3enkA 1.9a crystal structure of udp-glucose 4-epimerase from burkholderia pseudomallei
44% identity, 98% coverage: 6:330/332 of query aligns to 2:334/340 of 3enkA
- active site: S127 (= S124), S128 (≠ T125), T130 (≠ A127), Y152 (= Y149), K156 (= K153)
- binding nicotinamide-adenine-dinucleotide: G11 (= G15), G14 (= G18), Y15 (= Y19), I16 (= I20), D35 (= D39), N36 (= N40), V38 (≠ S42), N39 (≠ T43), S40 (≠ G44), D62 (= D59), V63 (= V60), F84 (= F81), A85 (= A82), A86 (≠ G83), K88 (≠ I85), N103 (= N100), S126 (= S123), S128 (≠ T125), Y152 (= Y149), K156 (= K153), Y180 (= Y176), P183 (≠ V179)
- binding uridine-5'-diphosphate-glucose: T130 (≠ A127), N182 (= N178), N201 (≠ T196), N202 (≠ H197), L203 (= L198), R219 (≠ S214), V220 (≠ I215), F221 (= F216), R234 (= R229), Y236 (= Y231), V272 (= V267), R295 (= R290), D298 (= D293)
2cnbA Trypanosoma brucei udp-galactose-4-epimerase in ternary complex with NAD and the substrate analogue udp-4-deoxy-4- fluoro-alpha-d-galactose (see paper)
39% identity, 97% coverage: 10:330/332 of query aligns to 4:360/366 of 2cnbA
- active site: S144 (≠ T125), A145 (= A126), A146 (= A127), Y169 (= Y149), K173 (= K153)
- binding nicotinamide-adenine-dinucleotide: G9 (= G15), G12 (= G18), Y13 (= Y19), I14 (= I20), D34 (= D39), S35 (≠ N40), V37 (vs. gap), G38 (vs. gap), D77 (= D59), V78 (= V60), M100 (≠ F81), C101 (≠ A82), A102 (≠ G83), L104 (≠ I85), N119 (= N100), S143 (= S124), S144 (≠ T125), Y169 (= Y149), K173 (= K153), Y196 (= Y176), F197 (= F177), A199 (≠ V179)
- binding uridine-5'-diphosphate-4-deoxy-4-fluoro-alpha-d-galactose: L104 (≠ I85), S144 (≠ T125), Y169 (= Y149), F197 (= F177), N198 (= N178), H217 (= H197), L218 (= L198), P238 (≠ S214), I239 (= I215), F240 (= F216), C251 (= C227), R253 (= R229), V297 (= V267), R320 (= R290), D323 (= D293)
1gy8C Trypanosoma brucei udp-galactose 4' epimerase (see paper)
39% identity, 97% coverage: 10:330/332 of query aligns to 4:364/370 of 1gy8C
- active site: S144 (≠ T125), A145 (= A126), A146 (= A127), Y170 (= Y149), K174 (= K153)
- binding nicotinamide-adenine-dinucleotide: G9 (= G15), G12 (= G18), Y13 (= Y19), I14 (= I20), D34 (= D39), S35 (≠ N40), L36 (= L41), V37 (vs. gap), G38 (vs. gap), D77 (= D59), V78 (= V60), M100 (≠ F81), C101 (≠ A82), A102 (≠ G83), L104 (≠ I85), N119 (= N100), S142 (= S123), S143 (= S124), S144 (≠ T125), Y170 (= Y149), K174 (= K153), Y197 (= Y176), A200 (≠ V179)
- binding uridine-5'-diphosphate: N199 (= N178), H218 (= H197), L219 (= L198), I222 (≠ V201), M241 (≠ L213), P242 (≠ S214), I243 (= I215), F244 (= F216), C255 (= C227), R257 (= R229), R324 (= R290), D327 (= D293)
Query Sequence
>AZOBR_RS33555 FitnessBrowser__azobra:AZOBR_RS33555
MLDETATPHRVLVTGGAGYIGSHVLHALADAGIPAVTIDNLSTGRRAAVPASVPLVEGDV
GSAELLERVIRDHAVDAVMHFAGSIVVPESVEKPLAYYRNNTVNSLTLMDACVRLGVGNI
VFSSTAAVYGAPDRVPIDEATPTAPINPYGTSKLMTEQMLRDAGAAHGLRSVILRYFNVA
GADAAGRTGQATPTATHLIKVACQALLGRRPALSIFGTDYDTPDGTCIRDYIHVSDLADA
HVLALLHLRRGGESLTLNCGYGRGASVHEVVRTLEEVSGEKVPATLAPRRPGDPPQLVAK
ADRIRERLGWVPKHDRLDGIVRDALAWERSLT
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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