SitesBLAST
Comparing 3608830 FitnessBrowser__Dino:3608830 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)
3i6vA Crystal structure of a periplasmic his/glu/gln/arg/opine family- binding protein from silicibacter pomeroyi in complex with lysine
75% identity, 87% coverage: 26:236/242 of query aligns to 1:211/218 of 3i6vA
- binding lysine: E7 (= E32), Y10 (= Y35), W48 (= W73), G66 (= G91), M67 (= M92), S68 (= S93), R73 (= R98), Q107 (= Q133), T110 (= T136), I111 (= I137), Q112 (= Q138)
5itoA Structure of the periplasmic binding protein m117n-noct from a. Tumefaciens in complex with octopine (see paper)
31% identity, 88% coverage: 23:236/242 of query aligns to 1:249/255 of 5itoA
- binding octopine: E10 (= E32), Y13 (= Y35), W51 (= W73), A68 (= A90), A69 (≠ G91), G71 (≠ S93), R76 (= R98), Q139 (= Q133), T142 (= T136), S143 (≠ I137), H144 (≠ Q138), S181 (≠ D173)
5ovzA High resolution structure of the pbp noct in complex with nopaline (see paper)
31% identity, 88% coverage: 23:236/242 of query aligns to 1:249/259 of 5ovzA
- binding N-[(1S)-4-carbamimidamido-1-carboxybutyl]-D-glutamic acid: E10 (= E32), Y13 (= Y35), W51 (= W73), A68 (= A90), A69 (≠ G91), G71 (≠ S93), R76 (= R98), M91 (≠ S114), Q139 (= Q133), T142 (= T136), S143 (≠ I137), H144 (≠ Q138), S181 (≠ D173), V213 (≠ I200)
P02911 Lysine/arginine/ornithine-binding periplasmic protein; LAO-binding protein from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
31% identity, 97% coverage: 2:236/242 of query aligns to 3:253/260 of P02911
- D33 (≠ E32) binding ; binding ; binding ; mutation to A: Decreases arginine and histidine binding affinity.
- Y36 (= Y35) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- D52 (≠ E51) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- C60 (= C59) modified: Disulfide link with 67
- C67 (= C66) modified: Disulfide link with 60
- F74 (≠ W73) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- S91 (≠ A90) binding ; binding ; mutation to A: Has no effect on the arginine and histidine binding affinity.
- S92 (≠ G91) binding ; binding ; binding ; mutation to A: Decreases arginine and histidine binding affinity.
- S94 (= S93) binding ; binding ; binding ; mutation to A: Decreases arginine and histidine binding affinity.
- R99 (= R98) binding ; binding ; binding ; mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- L139 (≠ Q133) mutation to K: Changes ligand specificity. Can bind glutamine. Still able to bind basic amino acids, however, with 1000-fold less affinity for arginine.; mutation to Q: Does not affect ligand preference.
- T143 (≠ I137) binding ; binding ; binding
- D183 (= D173) binding ; binding ; mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
5otcA Structure of the periplasmic binding protein (pbp) noct from agrobacterium tumefaciens c58 in complex with noroctopinic acid. (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 3:248/256 of 5otcA
- binding (2~{S})-5-azanyl-2-(2-hydroxy-2-oxoethylamino)pentanoic acid: E9 (= E32), Y12 (= Y35), W50 (= W73), A68 (≠ G91), G70 (≠ S93), R75 (= R98), Q138 (= Q133), T141 (= T136), S142 (≠ I137), H143 (≠ Q138), S180 (≠ D173)
5otaA Structure of the periplasmic binding protein (pbp) noct from agrobacterium tumefaciens c58 in complex with octopinic acid (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 3:248/254 of 5otaA
- binding (2~{S})-5-azanyl-2-[[(2~{R})-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]pentanoic acid: E9 (= E32), Y12 (= Y35), W50 (= W73), A68 (≠ G91), G70 (≠ S93), R75 (= R98), M90 (≠ S114), Q138 (= Q133), T141 (= T136), S142 (≠ I137), H143 (≠ Q138), S180 (≠ D173)
5ot9A Structure of the periplasmic binding protein (pbp) noct from a.Tumefaciens c58 in complex with histopine. (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 3:248/254 of 5ot9A
- binding Histopine: E9 (= E32), Y12 (= Y35), W50 (= W73), A67 (= A90), A68 (≠ G91), R75 (= R98), M90 (≠ S114), Q138 (= Q133), T141 (= T136), S142 (≠ I137), H143 (≠ Q138), S180 (≠ D173)
4powA Structure of the pbp noct in complex with pyronopaline (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 3:248/254 of 4powA
- binding 1-[(1S)-4-carbamimidamido-1-carboxybutyl]-5-oxo-D-proline: E9 (= E32), Y12 (= Y35), W50 (= W73), A67 (= A90), A68 (≠ G91), G70 (≠ S93), R75 (= R98), M90 (≠ S114), Q138 (= Q133), T141 (= T136), S142 (≠ I137), H143 (≠ Q138), S180 (≠ D173)
4zv2A An ancestral arginine-binding protein bound to glutamine (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:223/225 of 4zv2A
5owfA Structure of a lao-binding protein mutant with glutamine (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 2:228/235 of 5owfA
4zv1A An ancestral arginine-binding protein bound to arginine (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:225/226 of 4zv1A
- binding arginine: E11 (= E32), F14 (≠ Y35), F52 (≠ W73), A69 (= A90), G70 (= G91), M71 (= M92), T72 (≠ S93), R77 (= R98), Q117 (= Q133), S120 (≠ T136), T121 (≠ I137), D161 (= D173)
1lstA Three-dimensional structures of the periplasmic lysine-, arginine-, ornithine-binding protein with and without a ligand (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:231/238 of 1lstA
1lahE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:231/238 of 1lahE
1lagE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:231/238 of 1lagE
- binding histidine: Y14 (= Y35), F52 (≠ W73), S69 (≠ A90), S70 (≠ G91), L71 (≠ M92), S72 (= S93), R77 (= R98), L117 (≠ Q133), S120 (≠ T136), Q122 (= Q138), D161 (= D173)
1lafE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
31% identity, 87% coverage: 26:236/242 of query aligns to 5:231/238 of 1lafE
- binding arginine: D11 (≠ E32), Y14 (= Y35), F52 (≠ W73), S69 (≠ A90), S70 (≠ G91), S72 (= S93), R77 (= R98), L117 (≠ Q133), S120 (≠ T136), T121 (≠ I137), Q122 (= Q138), D161 (= D173)
5orgA Structure of the periplasmic binding protein (pbp) occj from a. Tumefaciens b6 in complex with octopine. (see paper)
32% identity, 87% coverage: 26:236/242 of query aligns to 5:250/257 of 5orgA
- binding octopine: E11 (= E32), Y14 (= Y35), W52 (= W73), A69 (= A90), A70 (≠ G91), M71 (= M92), S72 (= S93), R77 (= R98), N92 (≠ D112), Q140 (= Q138), T143 (≠ H141), T144 (≠ I142), N183 (≠ D173)
P0AEU0 Histidine-binding periplasmic protein; HBP from Escherichia coli (strain K12) (see 3 papers)
31% identity, 87% coverage: 26:236/242 of query aligns to 27:253/260 of P0AEU0
- C60 (= C59) modified: Disulfide link with 67
- C67 (= C66) modified: Disulfide link with 60
- S91 (≠ A90) binding
- S92 (≠ G91) binding
- S94 (= S93) binding
- R99 (= R98) binding
- T143 (≠ I137) binding
- D183 (= D173) binding
Sites not aligning to the query:
P02910 Histidine-binding periplasmic protein; HBP from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
31% identity, 87% coverage: 27:236/242 of query aligns to 28:253/260 of P02910
- E40 (≠ N39) mutation to K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-47.
- K42 (≠ L41) mutation to E: Increases ATPase-inducing activity and histidine transport; when associated with K-47.
- E47 (= E46) mutation to K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-40. Increases ATPase-inducing activity and histidine transport; when associated with E-42.
- D171 (≠ A161) mutation D->A,N: Strong decrease in ATPase-inducing activity and histidine transport.
- R176 (≠ E166) mutation R->D,S: Strong decrease in ATPase-inducing activity and histidine transport.
- D178 (= D168) mutation to A: Slight decrease in ATPase-inducing activity and histidine transport.
Sites not aligning to the query:
1hslA Refined 1.89 angstroms structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport(slash)chemosensory receptors (see paper)
31% identity, 87% coverage: 27:236/242 of query aligns to 6:231/238 of 1hslA