SitesBLAST
Comparing 5208934 FitnessBrowser__PV4:5208934 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)
2v27B Structure of the cold active phenylalanine hydroxylase from colwellia psychrerythraea 34h (see paper)
61% identity, 94% coverage: 17:277/277 of query aligns to 2:264/272 of 2v27B
1ltvA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure with bound oxidized fe(iii) (see paper)
48% identity, 79% coverage: 27:245/277 of query aligns to 23:242/275 of 1ltvA
1ltzA Crystal structure of chromobacterium violaceum phenylalanine hydroxylase, structure has bound iron (iii) and oxidized cofactor 7, 8-dihydrobiopterin (see paper)
48% identity, 79% coverage: 27:245/277 of query aligns to 25:244/274 of 1ltzA
4etlA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum f258a mutation (see paper)
48% identity, 79% coverage: 27:245/277 of query aligns to 25:244/277 of 4etlA
3tcyA Crystallographic structure of phenylalanine hydroxylase from chromobacterium violaceum (cpah) bound to phenylalanine in a site distal to the active site (see paper)
48% identity, 79% coverage: 27:245/277 of query aligns to 25:244/277 of 3tcyA
Sites not aligning to the query:
5jk5A Phenylalanine hydroxylase from dictyostelium - bh2 complex
39% identity, 80% coverage: 30:250/277 of query aligns to 151:374/400 of 5jk5A
- active site: H259 (= H134), H264 (= H139), E304 (= E179), S323 (= S199)
- binding fe (iii) ion: H259 (= H134), H264 (= H139), E304 (= E179)
- binding 7,8-dihydrobiopterin: G221 (≠ A96), L222 (= L97), L223 (≠ I98), F228 (= F103), L229 (≠ F104), S296 (≠ A171), Y299 (= Y174)
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): T212 (= T87), P271 (= P146), D275 (≠ R150), R374 (≠ K250)
5jk8A Phenylalanine hydroxylase from dictyostelium - bh2, norleucine complex
39% identity, 80% coverage: 30:250/277 of query aligns to 142:365/390 of 5jk8A
- active site: H250 (= H134), H255 (= H139), E295 (= E179), S314 (= S199)
- binding fe (iii) ion: H250 (= H134), H255 (= H139), E295 (= E179)
- binding 7,8-dihydrobiopterin: L214 (≠ I98), A216 (≠ F100), F219 (= F103), S287 (≠ A171), Y290 (= Y174)
- binding norleucine: Y242 (= Y126), T243 (≠ L127), H250 (= H134), S314 (= S199), S315 (= S200)
- binding piperazine-n,n'-bis(2-ethanesulfonic acid): T203 (= T87), R226 (≠ Q110), D266 (≠ R150), R365 (≠ K250)
Sites not aligning to the query:
P90986 Tyrosine 3-monooxygenase; Abnormal catecholamine distribution protein 2; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Caenorhabditis elegans (see 4 papers)
35% identity, 80% coverage: 22:242/277 of query aligns to 231:454/519 of P90986
Sites not aligning to the query:
- 35 modified: Phosphoserine; by PKA
- 276:519 mutation Missing: In e1112; spontaneously induces activation of the crh-1/CREB1 transcription factor in cholinergic SIA neurons in the absence and presence of food. Reduces swimming-induced paralysis in response to amphetamine. Defective male mating behavior.
P04177 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Rattus norvegicus (Rat) (see 7 papers)
38% identity, 77% coverage: 30:243/277 of query aligns to 223:439/498 of P04177
- Q310 (≠ P113) mutation to H: Does not affect Vmax for phenylalanine. Increases KM for phenylalanine.
- H323 (≠ Y126) mutation to Y: Does not affect Vmax for phenylalaninet. Increases KM for phenylalanine.
- H331 (= H134) binding
- H336 (= H139) binding
- W372 (= W175) mutation to F: Does not affect substrate specificity.
- E376 (= E179) binding
- D425 (≠ I229) Important for substrate specificity; mutation to V: Shifts substrate specificity from tyrosine to phenylalanine.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 19 modified: Phosphoserine; by CaMK2
- 31 modified: Phosphoserine
- 40 modified: Phosphoserine; by CaMK2 and PKA
P17289 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Bos taurus (Bovine) (see 2 papers)
37% identity, 77% coverage: 30:241/277 of query aligns to 216:430/491 of P17289
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 19 modified: Phosphoserine; by CaMK2
- 31 modified: Phosphoserine
- 40 modified: Phosphoserine; by CaMK2 and PKA
2tohA Tyrosine hydroxylase catalytic and tetramerization domains from rat (see paper)
37% identity, 77% coverage: 30:243/277 of query aligns to 61:277/336 of 2tohA
- active site: H169 (= H134), H174 (= H139), E214 (= E179), S233 (= S199)
- binding fe (iii) ion: H169 (= H134), H174 (= H139), E214 (= E179)
- binding 7,8-dihydrobiopterin: V129 (= V94), L132 (= L97), L133 (≠ I98), Y138 (≠ F103), P165 (= P130), E170 (= E135), Y209 (= Y174)
6zn2A Partial structure of tyrosine hydroxylase in complex with dopamine showing the catalytic domain and an alpha-helix from the regulatory domain involved in dopamine binding. (see paper)
35% identity, 82% coverage: 16:242/277 of query aligns to 46:275/335 of 6zn2A
2xsnA Crystal structure of human tyrosine hydroxylase catalytic domain
35% identity, 82% coverage: 16:242/277 of query aligns to 47:276/335 of 2xsnA
6zvpD Atomic model of the em-based structure of the full-length tyrosine hydroxylase in complex with dopamine (residues 40-497) in which the regulatory domain (residues 40-165) has been included only with the backbone atoms (see paper)
35% identity, 82% coverage: 16:242/277 of query aligns to 169:398/458 of 6zvpD
Sites not aligning to the query:
P07101 Tyrosine 3-monooxygenase; Tyrosine 3-hydroxylase; TH; EC 1.14.16.2 from Homo sapiens (Human) (see 32 papers)
35% identity, 82% coverage: 16:242/277 of query aligns to 239:468/528 of P07101
- A241 (≠ T18) to T: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1260455415
- H246 (≠ L23) to Y: in ARSEGS; loss of about 40% of tyrosine 3-monooxygenase activity
- G247 (≠ P24) to S: in ARSEGS; loss of about 50% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs762304556
- E259 (= E36) to G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
- T276 (≠ H53) to P: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934581
- P301 (= P74) to A: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
- F309 (≠ V82) to S: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
- T314 (= T87) to M: in ARSEGS; parkinsonian symptoms in infancy; loss of about 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917764
- R319 (≠ A92) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
- R328 (≠ E101) to W: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs1428589694
- R337 (≠ Q110) to H: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs28934580
- C359 (≠ I132) to F: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs121917765
- F375 (= F148) to L: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs763198914
- A376 (= A149) to V: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
- L387 (= L160) to M: in ARSEGS; no effect on tyrosine 3-monooxygenase activity
- I394 (≠ R167) to T: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
- T399 (≠ R172) to M: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs1057520384
- Q412 (= Q185) to K: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; reduced affinity for L-tyrosine; dbSNP:rs121917762
- G414 (≠ D188) to R: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs370962049
- G428 (= G202) to R: in ARSEGS; phenotype with prominent levodopa-responsive myoconus-dystonia (M-D); dbSNP:rs1264884607
- R441 (≠ K215) to P: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs367874223
- S467 (= S241) to G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity
Sites not aligning to the query:
- 19 modified: Phosphoserine; by CaMK2; S → C: found in a patient with ARSEGS; uncertain significance; dbSNP:rs766704202
- 62 modified: Phosphoserine; S→A: Affects subcellular localization. Accumulates mainly in the soma of the neuroblastoma cells.; S→E: Does not affect subcellular localization. Distributed throughout the soma and neurites.
- 71 modified: Phosphoserine; by CaMK2 and PKA; S→E: Suppresses feedback inhibition induced by dopamine. Suppresses feedback inhibition induced by dopamine; when associated with A-207.
- 112 V → M: in dbSNP:rs6356
- 207 C → Y: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; C→A: Suppresses the decrease in tyrosine 3-monooxygenase activity induced by NEM modification. Suppresses feedback inhibition induced by dopamine; when associated with E-71.
- 227 D → G: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
- 233 R → H: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; shifted substrate specificity from tyrosine to phenylalanine and Dopa; dbSNP:rs80338892
- 236 L → P: in ARSEGS; severe parkinsonian symptoms in early infancy; strongly reduced stability and tyrosine 3-monooxygenase activity; rare mutation; dbSNP:rs121917763
- 492 P → L: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity; dbSNP:rs767635052
- 494 T → M: in ARSEGS; parkinsonian symptoms in infancy; no effect on tyrosine 3-monooxygenase activity; dbSNP:rs45471299
- 498 D → G: in ARSEGS; loss of over 80% of tyrosine 3-monooxygenase activity; dbSNP:rs771351747
- 499 V → M: in dbSNP:rs1800033
- 510 L → Q: in ARSEGS; complete loss of tyrosine 3-monooxygenase activity
P16331 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Mus musculus (Mouse) (see paper)
36% identity, 80% coverage: 30:250/277 of query aligns to 177:400/453 of P16331
- F263 (= F112) mutation to S: Mutant mice have features of phenylketonuria.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 106 V→A: Mutant mice have mild features of phenylketonuria.
P00439 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Homo sapiens (Human) (see 43 papers)
37% identity, 80% coverage: 30:250/277 of query aligns to 177:400/452 of P00439
- V177 (≠ I30) to L: in PKU; haplotype 6; dbSNP:rs199475602
- E178 (≠ Q31) to G: in non-PKU HPA; dbSNP:rs77958223
- V190 (≠ L43) to A: in PKU; haplotype 3; dbSNP:rs62514919
- H201 (≠ Y54) to Y: in non-PKU HPA; haplotype 1; dbSNP:rs62517205
- Y204 (≠ D57) to C: in PKU; mild; haplotypes 3,4; dbSNP:rs62514927
- N207 (vs. gap) to S: in PKU; severe; haplotype 4; dbSNP:rs62508721
- P211 (≠ K61) to T: in PKU; haplotype 4; dbSNP:rs62514931
- L213 (= L63) to P: in PKU; severe; dbSNP:rs62516109
- G218 (≠ A67) to V: in PKU; haplotypes 1,2; dbSNP:rs62514933
- E221 (≠ A70) to G: in PKU; haplotype 4; dbSNP:rs62514934
- D222 (= D71) to V: in PKU; haplotypes 3,4; dbSNP:rs62507319
- I224 (= I73) to M: in PKU; haplotype 4; dbSNP:rs199475576
- P225 (= P74) to T: in PKU; haplotype 1; dbSNP:rs199475589
- V230 (≠ I79) to I: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62516152
- F233 (≠ V82) to L: in PKU; haplotypes 2,3; dbSNP:rs62517208
- T238 (= T87) to P: in PKU; haplotype 4; dbSNP:rs199475577
- R241 (≠ K90) to C: in non-PKU HPA and PKU; haplotype 34; dbSNP:rs76687508; to H: in PKU; haplotypes 1,5; dbSNP:rs62508730
- R243 (≠ A92) to Q: in non-PKU HPA and PKU; haplotypes 4,7,9; dbSNP:rs62508588
- P244 (≠ A93) to L: in PKU; haplotype 12; dbSNP:rs118203923
- V245 (= V94) to A: in PKU, HPA and non-PKU HPA; haplotypes 3,7; dbSNP:rs796052017; to E: in PKU; haplotype 11; dbSNP:rs76212747
- G247 (≠ A96) to V: in PKU; haplotype 4; dbSNP:rs199475579
- L249 (≠ I98) to F: in PKU; haplotype 1; dbSNP:rs74503222
- R252 (≠ E101) to G: in PKU; haplotype 7; dbSNP:rs5030847; to Q: in PKU; haplotype 1; dbSNP:rs62644503; to W: in PKU; haplotypes 1,6,7,8,42, 69; complete loss of activity; dbSNP:rs5030847
- L255 (≠ F104) to S: in PKU; haplotype 36; dbSNP:rs62642930; to V: in PKU; haplotypes 18,21; dbSNP:rs62642931
- A259 (= A108) to T: in PKU; haplotype 3; dbSNP:rs62642932; to V: in PKU; haplotypes 7,42; dbSNP:rs118203921
- R261 (≠ Q110) to Q: in HPA and PKU; mild; haplotypes 1,2,4,22, 24,28; dbSNP:rs5030849
- I269 (= I118) to L: in non-PKU HPA; dbSNP:rs62508692
- R270 (= R119) to S: in PKU; haplotype 1; dbSNP:rs62514951
- S273 (≠ E122) to F: in PKU; haplotype 7; dbSNP:rs62514953
- P275 (≠ F124) to L: in PKU; reduced activity; increased affinity for the substrate; mildly reduced substrate activation; decreased cofactor affinity; dbSNP:rs62508715
- M276 (≠ D125) to V: in PKU; haplotype 4; dbSNP:rs62516149
- Y277 (= Y126) to D: in PKU; haplotype 2; dbSNP:rs78655458
- E280 (= E129) to K: in PKU; haplotypes 1,2,4,16,38; partial residual activity; dbSNP:rs62508698
- P281 (= P130) to L: in PKU; haplotypes 1,4; dbSNP:rs5030851
- D282 (= D131) to N: in PKU; haplotype 1; dbSNP:rs199475582
- I283 (= I132) to F: in PKU; haplotype 21; dbSNP:rs62517168; to N: in PKU; severe; dbSNP:rs62508693; mutation to C: Loss of positive cooperativity and reduction of fold-activation by L-Phe preincubation.
- R297 (≠ P146) to C: in PKU; haplotype 4; dbSNP:rs62642945
- F299 (= F148) to C: in PKU; haplotype 8; dbSNP:rs62642933
- A300 (= A149) to S: in PKU and HPA; haplotype 1; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030853
- S303 (= S152) to P: in PKU; haplotype 5; dbSNP:rs199475608
- I306 (≠ Y155) to V: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642934
- A309 (≠ L158) to D: in PKU; haplotype 7; dbSNP:rs62642935
- S310 (≠ G159) to F: in PKU; haplotype 7; dbSNP:rs62642913; to Y: in HPA; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62642913
- L311 (= L160) to P: in PKU; haplotypes 1,7,10; dbSNP:rs62642936
- P314 (≠ S163) to S: in HPA; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs199475650
- I318 (≠ R167) to T: in PKU; partial loss of activity; dbSNP:rs62642918
- A322 (= A171) to G: in PKU; haplotype 12; dbSNP:rs62514958; to T: in PKU; haplotype 1; dbSNP:rs62514957
- F331 (= F180) to L: in PKU; haplotype 1; dbSNP:rs62517179
- D338 (= D188) to Y: in PKU; haplotype 4; dbSNP:rs62516150
- A342 (≠ I192) to T: in PKU; haplotype 5; dbSNP:rs62507282
- A345 (≠ G195) to T: in PKU; haplotype 7; dbSNP:rs62516062
- L348 (= L198) to V: in PKU; mild haplotype 9; dbSNP:rs62516092
- S349 (= S199) to L: in PKU; severe; dbSNP:rs62507279; to P: in PKU; haplotypes 1,4; dbSNP:rs62508646
- S350 (= S200) to T: in PKU; haplotype 2; dbSNP:rs62517183
- L364 (≠ V214) natural variant: Missing (in PKU; haplotype 5; dbSNP:rs62516096)
- Y377 (= Y227) to C: in PKU; haplotype 4; dbSNP:rs62642942
- T380 (≠ D230) to M: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs62642937
- Y387 (= Y237) to H: in PKU; haplotype 1; dbSNP:rs62517194
- V388 (≠ A238) to M: in PKU; haplotypes 1,4; dbSNP:rs62516101
- E390 (≠ D240) to G: in PKU and non-PKU HPA; haplotype 4; dbSNP:rs5030856
- A395 (≠ L245) to P: in PKU; haplotype 1; dbSNP:rs62516103
Sites not aligning to the query:
- 16 modified: Phosphoserine; by PKA; S → P: in PKU; uncertain significance; dbSNP:rs62642946
- 39 F → L: in HPA and PKU; haplotype 1; dbSNP:rs62642926; natural variant: Missing (in PKU; haplotypes 9,21)
- 41 L → P: in PKU; mild; dbSNP:rs62642916
- 42 K → I: in PKU; haplotype 21; dbSNP:rs62635346
- 46 G → S: in PKU; haplotype 5; significantly reduces phenylalanine binding; dbSNP:rs74603784
- 47 A → V: in non-PKU HPA; haplotype 4; significantly reduces phenylalanine binding; dbSNP:rs118203925
- 48 L → S: in PKU; mild; haplotypes 3,4; dbSNP:rs5030841
- 55 F → L: in HPA and PKU; does not affect oligomerization; results in loss of substrate activation; dbSNP:rs199475598
- 56 E → D: in PKU; haplotype 10; dbSNP:rs199475567
- 63:64 natural variant: TH -> PN (in PKU; haplotype 1; abolishes phenylalanine binding)
- 65 I → S: in PKU; results in disturbed oligomerization; results in loss of substrate activation; dbSNP:rs75193786; I → T: in PKU; haplotypes 1,5,9,21,B; abolishes phenylalanine binding; dbSNP:rs75193786; I → V: in HPA and PKU; dbSNP:rs199475643
- 67 S → P: in PKU; haplotype 4; dbSNP:rs5030842
- 68 R → S: in PKU; haplotype 1; dbSNP:rs76394784
- 76 E → G: in non-PKU HPA; dbSNP:rs62507347
- 84 D → Y: in PKU; haplotype 4; dbSNP:rs62514902
- 87 S → R: in non-PKU HPA; haplotype 1; dbSNP:rs62516151
- 94 natural variant: Missing (in PKU; mild; haplotype 2)
- 98 L → S: in non-PKU HPA; dbSNP:rs62517167
- 104 A → D: in PKU; mild; haplotype 1; dbSNP:rs62642929
- 124 T → I: in PKU; haplotype 28; dbSNP:rs199475571
- 143 D → G: in PKU; haplotype 11; dbSNP:rs199475572
- 148 G → S: in PKU; haplotypes 1,2,7; dbSNP:rs80297647
- 151 D → H: in PKU; haplotypes 1,8; dbSNP:rs199475597
- 157 R → N: in PKU; severe; 5% activity; requires 2 nucleotide substitutions; dbSNP:rs1565853495
- 158 R → Q: in PKU; haplotypes 1,2,4,7,16, 28; dbSNP:rs5030843
- 161 F → S: in PKU; haplotype 4; dbSNP:rs79635844
- 164 I → T: in PKU; haplotype 1; dbSNP:rs199475595
- 170 H → Q: in PKU; does not affect oligomerization; dbSNP:rs199475652
- 171 G → A: in PKU; haplotype 1; dbSNP:rs199475596
- 173 P → T: in PKU; haplotype 4; dbSNP:rs199475574
- 174 I → T: in PKU; haplotype 1; dbSNP:rs138809906
- 176 R → L: in non-PKU HPA and PKU; dbSNP:rs74486803
- 403 A → V: in non-PKU HPA and PKU; haplotype 43; dbSNP:rs5030857
- 408 R → Q: in PKU; haplotypes 4,12; dbSNP:rs5030859; R → W: in HPA and PKU; haplotypes 1,2,4,5,13,34,41,44; most common mutation; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030858
- 410 F → S: in PKU; mild; dbSNP:rs62644475
- 413 R → P: in non-PKU HPA and PKU; haplotype 4; dbSNP:rs79931499; R → S: in PKU; haplotype 1; dbSNP:rs62644467
- 414 Y → C: in HPA and PKU; haplotype 4; does not affect oligomerization; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs5030860
- 415 D → N: in PKU, HPA and non-PKU HPA; haplotype 1; dbSNP:rs62644499
- 417 Y → H: in PKU; reduction in activity is probably due to a global conformational change in the protein that reduces allostery; dbSNP:rs62644471
- 418 T → P: in PKU; haplotype 4; dbSNP:rs62644501
P04176 Phenylalanine-4-hydroxylase; PAH; Phe-4-monooxygenase; EC 1.14.16.1 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 80% coverage: 30:250/277 of query aligns to 177:400/453 of P04176
- H285 (= H134) binding
- H290 (= H139) binding
- E330 (= E179) binding
Sites not aligning to the query:
- 16 modified: Phosphoserine; by PKA
5fgjA Structure of tetrameric rat phenylalanine hydroxylase, residues 1-453 (see paper)
36% identity, 80% coverage: 30:250/277 of query aligns to 155:378/428 of 5fgjA
1kw0A Catalytic domain of human phenylalanine hydroxylase (fe(ii)) in complex with tetrahydrobiopterin and thienylalanine (see paper)
37% identity, 80% coverage: 30:250/277 of query aligns to 60:283/307 of 1kw0A
- active site: H168 (= H134), H173 (= H139), E213 (= E179), S232 (= S199)
- binding fe (ii) ion: H168 (= H134), H173 (= H139), E213 (= E179)
- binding 5,6,7,8-tetrahydrobiopterin: L131 (= L97), L132 (≠ I98), S134 (≠ F100), F137 (= F103), H147 (≠ P113), E169 (= E135), E213 (= E179)
- binding beta(2-thienyl)alanine: R153 (= R119), Y160 (= Y126), T161 (≠ L127), E163 (= E129), P164 (= P130), H168 (= H134), F214 (= F180), S232 (= S199), S233 (= S200)
Query Sequence
>5208934 FitnessBrowser__PV4:5208934
MEAGAVICVVFIMSKQTTYQARLPDSQGVIQYPDNEHEIWQALYDRQKGNLPHYACDAYL
KGLEDLALPADRIPQLGEIDAVLQQATGWKTAAVPALISFEKFFQLLANQEFPVATFIRS
KEEFDYLQEPDIFHEIFGHCPLLTNPSFARFSHEYGKLGLAASKEERVFLARLYWFTVEF
GLIRQTNDELKIYGGGILSSPGETLYAMSDTPVVKPFDLLDILRTPYRIDIMQPIYYAID
SIDYLDEIVKMDIMGAVTKARQLGLHAPMFEPKSKAS
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