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* Residue conservation analysis
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PDB id:
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Ligase
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Title:
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Protein crystal growth improvement leading to the 2.5a crystallographic structure of ubiquitin-conjugating enzyme (ubc-1) from caenorhabditis elegans
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Structure:
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Ubiquitin-conjugating enzyme e2 1. Chain: a. Synonym: ubiquitin-protein ligase 1, ubiquitin carrier protein 1. Engineered: yes
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Source:
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Caenorhabditis elegans. Organism_taxid: 6239. Gene: ubc-1. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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2.50Å
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R-factor:
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0.242
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R-free:
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0.273
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Authors:
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J.A.Gavira,E.Digiammarino,W.Tempel,D.Toh,Z.J.Liu,B.C.Wang, E.Meehan,J.D.Ng,Southeast Collaboratory For Structural Genomics (Secsg)
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Key ref:
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J.A.Gavira
et al.
Protein crystal growth improvement leading to the 2.5a crystallographic structure of ubiquitin-Conjugating enzyme (ubc-1) from caenorhabditis elegans.
To be published,
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Date:
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11-Mar-05
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Release date:
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22-Mar-05
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PROCHECK
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Headers
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References
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P52478
(UBC1_CAEEL) -
Ubiquitin-conjugating enzyme E2 1
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Seq: Struc:
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192 a.a.
151 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.6.3.2.19
- Ubiquitin--protein ligase.
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Reaction:
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ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
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ATP
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ubiquitin
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protein lysine
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=
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AMP
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+
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diphosphate
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+
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protein N-ubiquityllysine
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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regulation of protein metabolic process
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2 terms
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Biochemical function
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small conjugating protein ligase activity
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1 term
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