SitesBLAST
Comparing GFF4108 FitnessBrowser__WCS417:GFF4108 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)
3x43A Crystal structure of o-ureido-l-serine synthase (see paper)
42% identity, 99% coverage: 2:303/304 of query aligns to 2:300/316 of 3x43A
- active site: K42 (= K43), S264 (= S267)
- binding pyridoxal-5'-phosphate: K42 (= K43), N72 (= N75), F175 (≠ I179), G176 (= G180), T177 (= T181), T178 (≠ G182), T180 (≠ H184), G220 (= G223), S264 (= S267), P290 (≠ Y293), D291 (= D294)
D2Z027 O-ureido-L-serine synthase; Cysteine synthase homolog DscD; O-acetylserine sulfhydrylase; EC 2.6.99.3; EC 2.5.1.47 from Streptomyces lavendulae (see paper)
42% identity, 99% coverage: 2:303/304 of query aligns to 3:301/324 of D2Z027
- K43 (= K43) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
- V74 (≠ T76) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
- Y97 (= Y99) mutation to F: KM for OAS is unchanged, KM for H(2)S is 0.073 mM.; mutation to M: KM for OAS is 330 mM, KM for H(2)S is 0.084.
- S121 (≠ N123) mutation to A: KM for OAS is 140 mM, KM for H(2)S is 0.095 mM.; mutation to M: KM for OAS is 44 mM, KM for H(2)S is 0.20 mM.
3x44A Crystal structure of o-ureido-l-serine-bound k43a mutant of o-ureido- l-serine synthase (see paper)
42% identity, 99% coverage: 2:303/304 of query aligns to 2:300/321 of 3x44A
- active site: A42 (≠ K43), S264 (= S267)
- binding (E)-O-(carbamoylamino)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: T69 (≠ S72), S70 (≠ G73), N72 (= N75), V73 (≠ T76), S120 (≠ N123), Q141 (= Q145), F175 (≠ I179), G176 (= G180), T177 (= T181), T178 (≠ G182), T180 (≠ H184), G220 (= G223), L221 (= L224), P223 (≠ I226), S264 (= S267), P290 (≠ Y293), D291 (= D294)
2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
41% identity, 96% coverage: 9:300/304 of query aligns to 6:296/302 of 2efyA
- active site: K40 (= K43), S70 (≠ G73), E200 (= E205), S204 (≠ C209), S263 (= S267)
- binding 5-oxohexanoic acid: T69 (≠ S72), G71 (= G74), T73 (= T76), Q141 (= Q145), G175 (= G180), G219 (= G223), M220 (≠ L224), P222 (≠ I226)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N75), Y172 (≠ C177), G175 (= G180), T176 (= T181), G177 (= G182), T179 (≠ H184), G219 (= G223), S263 (= S267), P289 (≠ Y293), D290 (= D294)
2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
41% identity, 96% coverage: 9:300/304 of query aligns to 6:296/302 of 2ecqA
- active site: K40 (= K43), S70 (≠ G73), E200 (= E205), S204 (≠ C209), S263 (= S267)
- binding (3s)-3-hydroxybutanoic acid: K40 (= K43), G71 (= G74), T73 (= T76), Q141 (= Q145), G219 (= G223)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N75), Y172 (≠ C177), G173 (= G178), G175 (= G180), T176 (= T181), T179 (≠ H184), G219 (= G223), S263 (= S267), P289 (≠ Y293)
2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
41% identity, 96% coverage: 9:300/304 of query aligns to 6:296/302 of 2ecoA
- active site: K40 (= K43), S70 (≠ G73), E200 (= E205), S204 (≠ C209), S263 (= S267)
- binding 4-methyl valeric acid: K40 (= K43), T69 (≠ S72), G71 (= G74), T73 (= T76), Q141 (= Q145), G175 (= G180), T176 (= T181), G219 (= G223)
- binding pyridoxal-5'-phosphate: K40 (= K43), N72 (= N75), Y172 (≠ C177), G175 (= G180), T176 (= T181), T179 (≠ H184), G219 (= G223), S263 (= S267), P289 (≠ Y293), D290 (= D294)
4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
36% identity, 98% coverage: 6:303/304 of query aligns to 38:341/486 of 4pcuA
- active site: K77 (= K43), S105 (≠ G73), D237 (≠ E205), S305 (= S267)
- binding protoporphyrin ix containing fe: A182 (≠ G149), P185 (= P152), L186 (≠ Q153), Y189 (≠ R156), R222 (≠ E190), T269 (≠ S231)
- binding pyridoxal-5'-phosphate: K77 (= K43), N107 (= N75), G212 (= G180), T213 (= T181), G214 (= G182), T216 (≠ H184), G261 (= G223), S305 (= S267), P331 (≠ Y293), D332 (= D294)
Sites not aligning to the query:
- binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
- binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479
7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
36% identity, 98% coverage: 6:303/304 of query aligns to 40:345/500 of 7qgtB
- binding protoporphyrin ix containing fe: A186 (≠ G149), P189 (= P152), L190 (≠ Q153), Y193 (≠ R156), R226 (≠ E190)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K43), T106 (≠ S72), S107 (≠ G73), N109 (= N75), T110 (= T76), Q182 (= Q145), G216 (= G180), T217 (= T181), G218 (= G182), T220 (≠ H184), G265 (= G223), S309 (= S267), P335 (≠ Y293), D336 (= D294)
Sites not aligning to the query:
7qgtA Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
36% identity, 98% coverage: 6:303/304 of query aligns to 40:345/500 of 7qgtA
- binding protoporphyrin ix containing fe: A186 (≠ G149), P189 (= P152), L190 (≠ Q153), Y193 (≠ R156), R226 (≠ E190)
- binding pyridoxal-5'-phosphate: K79 (= K43), N109 (= N75), G216 (= G180), T217 (= T181), G218 (= G182), T220 (≠ H184), G265 (= G223), S309 (= S267), P335 (≠ Y293), D336 (= D294)
Sites not aligning to the query:
5xenA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-serine-plp schiff base
39% identity, 98% coverage: 2:300/304 of query aligns to 2:300/300 of 5xenA
- binding pyridoxal-5'-phosphate: K42 (= K43), K42 (= K43), N72 (= N75), N72 (= N75), T175 (≠ I179), T175 (≠ I179), G176 (= G180), G176 (= G180), T177 (= T181), T177 (= T181), G178 (= G182), G178 (= G182), S180 (≠ H184), S180 (≠ H184), G220 (vs. gap), G220 (vs. gap), S266 (= S267), S266 (= S267), T293 (≠ Y293), T293 (≠ Y293), D294 (= D294), D294 (= D294)
- binding serine: K42 (= K43), T69 (≠ S72), S70 (≠ G73), N72 (= N75), T73 (= T76), Q142 (= Q145)
5xemA Crystal structure of a hydrogen sulfide-producing enzyme (fn1220) from fusobacterium nucleatum in complex with l-lanthionine-plp schiff base
39% identity, 98% coverage: 2:300/304 of query aligns to 2:300/302 of 5xemA
- binding (2R)-2-azanyl-3-[(2R)-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-propanoic acid: K42 (= K43), T69 (≠ S72), S70 (≠ G73), N72 (= N75), T73 (= T76), M120 (≠ N123), Q142 (= Q145), G176 (= G180), T177 (= T181), G220 (vs. gap), M221 (vs. gap), G222 (= G223), S224 (= S225)
- binding calcium ion: L300 (= L300)
- binding pyridoxal-5'-phosphate: K42 (= K43), N72 (= N75), T175 (≠ I179), G176 (= G180), T177 (= T181), G178 (= G182), S180 (≠ H184), G220 (vs. gap), S266 (= S267), T293 (≠ Y293), D294 (= D294)
Sites not aligning to the query:
P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
36% identity, 98% coverage: 6:303/304 of query aligns to 80:385/551 of P35520
- G85 (= G11) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
- T87 (= T13) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
- L101 (≠ I27) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
- K102 (vs. gap) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
- C109 (≠ L33) to R: in CBSD; loss of activity; dbSNP:rs778220779
- A114 (≠ P38) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
- K119 (= K43) modified: N6-(pyridoxal phosphate)lysine
- R125 (≠ G49) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
- M126 (= M50) to V: in CBSD; loss of activity
- E131 (= E55) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
- G139 (= G65) to R: in CBSD; mild form; dbSNP:rs121964965
- I143 (= I69) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
- E144 (= E70) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
- G148 (= G74) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
- N149 (= N75) binding
- L154 (= L80) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- A155 (≠ V81) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
- C165 (≠ V91) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
- M173 (≠ Y99) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
- E176 (= E102) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
- V180 (≠ L106) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
- T191 (vs. gap) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
- K211 (≠ Q134) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
- A226 (≠ G149) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
- N228 (= N151) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
- A231 (≠ T154) to P: in CBSD; has significantly decreased levels of enzyme activity
- D234 (= D157) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
- GTGGT 256:260 (≠ GTGGH 180:184) binding
- T257 (= T181) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
- T262 (= T186) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
- R266 (≠ E190) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
- K269 (= K193) natural variant: Missing (in CBSD; loss of expression)
- C272 (≠ W196) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
- C275 (≠ L199) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
- I278 (≠ M202) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
- D281 (≠ E205) to N: in CBSD; loss of activity
- A288 (vs. gap) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
- E302 (≠ H220) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
- G305 (= G223) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
- G307 (≠ S225) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
- V320 (≠ I238) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
- D321 (= D239) to V: in CBSD; loss of activity
- R336 (≠ K254) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
- L338 (≠ I256) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- G347 (= G265) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
- S349 (= S267) binding ; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- T353 (≠ N271) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
- R369 (≠ V287) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
- D376 (= D294) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
- R379 (≠ D297) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
- K384 (≠ G302) to E: in CBSD; severe form; dbSNP:rs121964967
Sites not aligning to the query:
- 18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
- 49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
- 52 binding axial binding residue
- 58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
- 65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
- 69 A → P: in dbSNP:rs17849313
- 78 P → R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
- 422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
- 427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
- 435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
- 439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
- 444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
- 449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
- 466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
- 500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
- 526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
- 539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
- 540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
- 548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989
3vbeC Crystal structure of beta-cyanoalanine synthase in soybean (see paper)
39% identity, 91% coverage: 6:283/304 of query aligns to 15:290/329 of 3vbeC
- active site: K52 (= K43), S81 (≠ G73), E212 (= E205), S216 (≠ C209), S275 (= S267)
- binding pyridoxal-5'-phosphate: K52 (= K43), N83 (= N75), M184 (≠ C177), G187 (= G180), S188 (≠ T181), G189 (= G182), T191 (≠ H184), G231 (= G223), S275 (= S267)
Sites not aligning to the query:
3pc4A Full length structure of cystathionine beta-synthase from drosophila in complex with serine (see paper)
36% identity, 98% coverage: 5:303/304 of query aligns to 42:348/504 of 3pc4A
- active site: K82 (= K43), S312 (= S267)
- binding protoporphyrin ix containing fe: A189 (≠ G149), P192 (= P152), L193 (≠ Q153), Y196 (≠ R156), R229 (≠ E190), T276 (≠ S231)
- binding (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine: K82 (= K43), T109 (≠ S72), S110 (≠ G73), N112 (= N75), T113 (= T76), Q185 (= Q145), A218 (≠ I179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (≠ H184), G268 (= G223), I269 (≠ L224), Y271 (≠ I226), S312 (= S267), P338 (≠ Y293), D339 (= D294)
Sites not aligning to the query:
3pc3A Full length structure of cystathionine beta-synthase from drosophila in complex with aminoacrylate (see paper)
36% identity, 98% coverage: 5:303/304 of query aligns to 42:348/504 of 3pc3A
- active site: K82 (= K43), S312 (= S267)
- binding protoporphyrin ix containing fe: A189 (≠ G149), P192 (= P152), L193 (≠ Q153), Y196 (≠ R156), R229 (≠ E190)
- binding 2-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]acrylic acid: K82 (= K43), T109 (≠ S72), S110 (≠ G73), N112 (= N75), T113 (= T76), Q185 (= Q145), A218 (≠ I179), G219 (= G180), T220 (= T181), A221 (≠ G182), T223 (≠ H184), G268 (= G223), I269 (≠ L224), S312 (= S267), P338 (≠ Y293), D339 (= D294)
Sites not aligning to the query:
3pc2A Full length structure of cystathionine beta-synthase from drosophila (see paper)
36% identity, 98% coverage: 5:303/304 of query aligns to 40:346/500 of 3pc2A
- active site: K80 (= K43), S310 (= S267)
- binding protoporphyrin ix containing fe: A187 (≠ G149), P190 (= P152), L191 (≠ Q153), Y194 (≠ R156), R227 (≠ E190)
- binding pyridoxal-5'-phosphate: K80 (= K43), N110 (= N75), A216 (≠ I179), G217 (= G180), T218 (= T181), A219 (≠ G182), T221 (≠ H184), G266 (= G223), S310 (= S267), P336 (≠ Y293), D337 (= D294)
Sites not aligning to the query:
Q9FS29 Bifunctional L-3-cyanoalanine synthase/cysteine synthase 2, mitochondrial; EC 2.5.1.47; EC 4.4.1.9 from Solanum tuberosum (Potato) (see paper)
39% identity, 91% coverage: 2:279/304 of query aligns to 28:304/347 of Q9FS29
- E157 (= E132) mutation E->N,Q: No effect on catalytic activities.
3vc3A Crystal structure of beta-cyanoalanine synthase k95a mutant in soybean (see paper)
39% identity, 93% coverage: 2:283/304 of query aligns to 4:283/322 of 3vc3A
- active site: A45 (≠ K43), S268 (= S267)
- binding n-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-cysteine: T73 (≠ S72), S74 (≠ G73), N76 (= N75), M77 (≠ T76), Q146 (= Q145), M177 (≠ C177), G180 (= G180), S181 (≠ T181), G182 (= G182), T184 (≠ H184), G224 (= G223), S268 (= S267)
Sites not aligning to the query:
Q2V0C9 Cystathionine beta-synthase; EC 4.2.1.22 from Apis mellifera (Honeybee) (see paper)
38% identity, 98% coverage: 6:303/304 of query aligns to 39:343/504 of Q2V0C9
- K78 (= K43) modified: N6-(pyridoxal phosphate)lysine
- N108 (= N75) binding
- GTGGT 215:219 (≠ GTGGH 180:184) binding
- S307 (= S267) binding
Sites not aligning to the query:
- 12 binding axial binding residue
- 23 binding axial binding residue
5ohxA Structure of active cystathionine b-synthase from apis mellifera (see paper)
38% identity, 98% coverage: 6:303/304 of query aligns to 35:336/488 of 5ohxA
- binding protoporphyrin ix containing fe: P181 (≠ G149), P184 (= P152), Y188 (≠ R156), R221 (≠ E190)
- binding pyridoxal-5'-phosphate: K74 (= K43), N104 (= N75), G209 (= G178), G211 (= G180), T212 (= T181), G213 (= G182), G214 (= G183), T215 (≠ H184), G256 (= G223), S300 (= S267), P326 (≠ Y293), D327 (= D294)
Sites not aligning to the query:
Query Sequence
>GFF4108 FitnessBrowser__WCS417:GFF4108
MLHNSILDVIGQTPIVRLAQFSEDLGIEVYAKLESLNPGGSHKARIALGMILDAERRGVL
IRDSGQTIIEPSGGNTGIGLVMAGNVLGYKVVLVIPDNYSPEKQKLLRLYGAKVVLSDSR
LGNNSHGEKCMELQLENPSYVMLNQQRNGANPQTHRDTTAPEILRAFGEKRADYFVCGIG
TGGHITGIGETLKTAWPELRVMGVEPEECDLLKNQHAPHHIQGLSIGLIPSILNLDVIDG
MLKVSRQDCIDMMKRIMRTDAISLGLSSAANMVAIARLAPELPPETVVLTMVYDNADSYL
PGFE
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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