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10 kDa heat shock protein, putative [Q4Q9D0]
Systematic NameLmjF.26.0640 [Leishmania major]
Gene NameLMJF_26_0640
Molecular Weight10609 Da
Protein Sequence Size100
Function
Charge2
Isoelectric Point9.8 pH
Description10 kDa heat shock protein, putative.
Subcellular Locationmitochondrial matrix[Predict]
E. C. Number N.A.
Sequence>tr|Q4Q9D0|Q4Q9D0_LEIMA 10 kDa heat shock protein, putative - Leishmania major
FRFTAPALKKLQPLGQRVLVKRMQAAKQTKAGILIPEQVAAKVNEGTVVAVAAGSKDWTP
TVKVGDTVLLPEYGGSSVKVDGEELVLYDESVLLGVLSS
DNA Sequence>LmjF26.0640 |||10 kDa heat shock protein, putative|Leishmania major|chr 26|||Manual
ATGTTCCGCT TCACCGCCCC CGCCCTGAAG AAGCTACAGC CGCTGGGCCA GCGCGTGCTGGTGAAGCGCA TGCAGGCGGC GAAGCAGACG AAGGCCGGCA TCCTGATCCC GGAGCAGGTGGCCGCCAAGG TCAACGAGGG CACCGTTGTG GCGGTGGCGG CTGGGTCGAA GGACTGGACGCCGACGGTGA AGGTGGGCGA CACGGTACTG CTGCCGGAGT ACGGCGGCTC TTCGGTGAAGGTGGACGGAG AGGAGCTCGT TCTGTACGAT GAGAGCGTGC TGCTTGGCGT GCTGTCAAGCTGA
10 kDa heat shock protein, putative Q4Q9D0]
Metabolite Information
Molecular FunctionATP binding; unfolded protein binding
Biochemical Pathwayprotein folding
Regulatory Pathway
KEGG PathwaysK04078
Orthologs
Homologs GI Percent Identity Evalue Score
Homo sapiensheat shock 10kDa protein 1 (chaperonin 10) [Homo sapiens]460.00000000000000277
DEG Information
DEG Protein DEG Organism Percent Identity Evalue Bit Score
YOR020c chaperonin, mitochondrialSaccharomyces cerevisiae38%0.0000000000000270.9
Post Translational Modification
PTM Type PTM Sub Type Score Modification Site Prosite ID
AcylationN-myristoylation site47-52; PS00008
PhosphorylationProtein kinase C phosphorylation site62-64; 78-80; PS00005
10 kDa heat shock protein, putative [Q4Q9D0]
Model Information
Template PDB ID1wnrG
Percent Identity40%
Target Region11-99
Template Region1-86
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
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/1918200/Q4Q9D0.pdb 2.0 89 = residues | | = | | Ramachandran plot: 95.9% core 4.1% allow 0.0% gener 0.0% = disall | | = | +| All Ramachandrans: 1 labelled residues (out of 87) = | +| Chi1-chi2 plots: 1 labelled residues (out of 43) = | | = | | Main-chain params: 6 better 0 inside 0 worse = | | Side-chain params: 5 better 0 inside 0 worse = | | = | *| Residue properties: Max.deviation: 2.2 Bad contacts: = 2 | *| Bond len/angle: 5.2 Morris et al class: 1 = 1 3 | | = | | G-factors Dihedrals: -0.12 Covalent: -0.33 Overall: = -0.19 | | = | | M/c bond lengths: 98.9% within limits 1.1% highlighted = | | M/c bond angles: 88.5% within limits 11.5% 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