LeishBase: Leishmania Structural Database
header
Home List of Proteins How to Visualize Structures Download Contact Us
Beta-tubulin [Q4Q4C4]
Systematic NameLmjF.33.0792 [Leishmania major]
Gene NameLMJF_33_0792
Molecular Weight49740 Da
Protein Sequence Size443
FunctionTubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a nonexchangeable site on the alpha-chain
Charge-21
Isoelectric Point4.4459 pH
DescriptionBeta-tubulin.
Subcellular Locationmicrotubule; protein complex[Predict]
E. C. Number N.A.
Sequence>tr|Q4Q4C4|Q4Q4C4_LEIMA Beta-tubulin - Leishmania major
REIVSCQAGQCGNQIGSKFWEVIADEHGVDPTGSYQGDSDLQLERINVYFDESAGGRYVP
RAVLMDLEPGTMDSVRAGPYGQLFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCR
KEAESCDCLQGFQLSHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVIPSPRVSDTVVE
PYNTTLSVHQLVENSDESMCIDNEALYDICFRTLKLTTPTFGDLNHLVAAVMSGVTCCLR
FPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVAELTQQMFDAKNMMQ
AADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFIEWIPNNIKSSICDIPPKGL
KMSVTFIGNNTCIQEMFRRVGEQFTGMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSE
YQQYQDATVEEEGEYDEEEEAY
DNA Sequence>LmjF33.0792 |||beta-tubulin|Leishmania major|chr 33|||Manual
ATGCGTGAGA TCGTTTCCTG CCAGGCCGGC CAGTGCGGCA ACCAGATCGG CTCTAAGTTTTGGGAGGTGA TTGCCGACGA ACATGGTGTC GATCCGACTG GCTCCTACCA GGGTGACTCGGATCTGCAGC TGGAGCGCAT CAACGTGTAC TTCGATGAGT CGGCGGGAGG CCGCTACGTGCCGCGCGCCG TGCTGATGGA CCTCGAGCCC GGCACTATGG ACTCCGTTCG CGCCGGCCCGTACGGCCAGC TGTTCCGCCC GGACAACTTC ATCTTTGGTC AGTCCGGCGC TGGCAACAACTGGGCCAAGG GCCACTACAC TGAGGGTGCG GAGCTGATCG ACTCCGTGCT TGATGTGTGCCGCAAGGAGG CGGAGAGCTG CGACTGCCTG CAGGGCTTCC AGCTGTCTCA CTCCCTCGGCGGCGGCACGG GCTCCGGCAT GGGCACGCTG CTCATTTCCA AGCTGCGCGA GGAGTACCCGGACCGGATCA TGATGACCTT CTCCGTCATC CCGTCCCCCC GCGTGTCGGA TACCGTTGTGGAGCCGTACA ACACGACCCT CTCTGTGCAC CAGCTCGTGG AGAACTCCGA CGAGTCCATGTGCATCGACA ACGAGGCGCT GTACGATATT TGCTTCCGCA CGCTGAAGCT GACGACGCCGACGTTCGGTG ACCTGAACCA CCTCGTCGCC GCTGTGATGT CTGGCGTGAC CTGCTGCCTGCGCTTCCCTG GCCAGCTGAA CTCTGACCTG CGCAAGCTTG CCGTGAACCT CGTGCCGTTCCCGCGCCTGC ACTTCTTCAT GATGGGCTTC GCGCCGCTGA CGAGCCGCGG CTCGCAGCAGTACCGCGGCC TGTCCGTCGC GGAGCTGACG CAGCAGATGT TCGACGCCAA GAACATGATGCAGGCCGCCG ACCCGCGCCA CGGCCGCTAC CTCACCGCGT CCGCGCTGTT CCGCGGCCGCATGTCGACCA AGGAGGTGGA CGAGCAGATG CTGAACGTGC AGAACAAGAA CTCCAGCTACTTCATCGAGT GGATCCCGAA CAACATCAAG TCGTCCATCT GCGATATCCC GCCCAAGGGTCTCAAGATGT CTGTCACCTT CATCGGCAAC AACACCTGCA TCCAGGAGAT GTTCCGCCGCGTCGGTGAGC AGTTCACGGG TATGTTCCGC CGCAAGGCCT TCCTCCACTG GTACACCGGTGAGGGCATGG ACGAGATGGA GTTCACGGAG GCCGAGTCCA ACATGAACGA CCTCGTCTCTGAGTACCAGC AGTACCAGGA CGCCACCGTC GAGGAGGAGG GCGAGTACGA CGAGGAGGAGGAAGCCTACT AG
Beta-tubulin Q4Q4C4]
Metabolite Informationcell motility; microtubule cytoskeleton organization and biogenesis; microtubule-based movement; protein polymerization
Molecular Function
Biochemical Pathway
Regulatory Pathway
KEGG PathwaysK07375
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapienstubulin, beta, 2 [Homo sapiens]820751
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
YFL037w beta-tubulinSaccharomyces cerevisiae68%0630
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
PDOC00595Formate--tetrahydrofolate ligase signatures184-187; 337-340; 370-373; PS00722
PDOC00199Tubulin subunits alpha, beta, and gamma signature140-146; PS00227
PDOC00200Tubulin-beta mRNA autoregulation signal1-4; PS00228
AcylationN-myristoylation site10-15; 13-18; 29-34; 34-39; 71-76; 93-98; 96-101; 98-103; 140-145; 141-146; 142-147; 144-149; 235-240; 244-249; 283-288; 360-365; 369-374; PS00008
GlycosylationN-glycosylation site184-187; 337-340; 370-373; PS00001
PhosphorylationCasein kinase II phosphorylation site115-118; 178-181; 221-224; 285-288; 322-325; 352-355; 409-412; 429-432; PS00006
PhosphorylationProtein kinase C phosphorylation site75-77; 172-174; 214-216; 274-276; 322-324; PS00005
SulfationTyrosine sulfation site43-57; 415-429; PS00003
Beta-tubulin [Q4Q4C4]
Model Information
Template PDB ID2hxhB
Percent Identity82%
Target Region1-443
Template Region2-426
Domain Information
Domains Start End
Active Site Information
Residue Active Site Number Functional Part
Co-Factor
Metal Description
Ligands
CAS number Name Mol. Weight Mol. Formula Smile Notation PDB Reference
58-64-0ADENOSINE-5'-DIPHOSPHATE427.201C10 H15 N5 O10 P2O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O2hxh
146-91-8GUANOSINE-5'-DIPHOSPHATE443.201C10 H15 N5 O11 P2O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O2hxh
86-01-1GUANOSINE-5'-TRIPHOSPHATE 523.18C10 H16 N5 O14 P3O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c2N=C(N)NC1=O)C(O)C3O2hxh
7791-18-6MAGNESIUM ION24.305Mg[Mg+2]2hxh
TAXOL853.906C47 H51 N O14O=C(c1ccccc1)NC(c2ccccc2)C(O)C(=O)OC5C(=C4C(OC(=O)C)C(=O)C7(C(C(OC(=O)c3ccccc3)C(O)(C4(C)C)C5)C6(OC(=O)C)C(OC6)CC7O)C)C2hxh
Mutational Information
Residue Feature Description
Modeled Protein Template Structure
+----------<<< P R O C H E C K S U M = M A R Y >>>----------+ | = | | /var/www/html/Services/SAVES_3/jobs/1793694/Q4Q4C4.pdb 2.0 443 = residues | | = | *| Ramachandran plot: 88.6% core 9.4% allow 1.3% gener 0.8% = disall | | = | *| All Ramachandrans: 23 labelled residues (out of 441) = | +| Chi1-chi2 plots: 2 labelled residues (out of 268) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 12.2 Bad contacts: = 15 | *| Bond len/angle: 7.0 Morris et al class: 1 = 1 3 | | = | | G-factors Dihedrals: -0.10 Covalent: -0.18 Overall: = -0.13 | | = | | M/c bond lengths: 99.1% within limits 0.9% highlighted = | | M/c bond angles: 93.0% within limits 7.0% highlighted = | | Planar groups: 100.0% within limits 0.0% highlighted = | | = | = +------------------------------------------------------------------------= ----+ + May be worth investigating further. * Worth investigating further.
Overlapped Structure Procheck Summary
LeishBase: Leishmania Structural Database