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PDBsum entry 2c4o

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protein ligands Protein-protein interface(s) links
Ligase PDB id
2c4o
Jmol
Contents
Protein chains
150 a.a. *
Ligands
SO4
GOL ×3
Waters ×262
* Residue conservation analysis
Superseded by: 2clw
PDB id:
2c4o
Name: Ligase
Title: Crystal structure of human ubiquitin-conjugating enzyme ubch5b
Structure: Ubiquitin-conjugating enzyme e2 d2. Chain: a. Synonym: ubiquitin-protein ligase d2, ubiquitin carrier protein d2, ubiquitin-conjugating enzyme e2-17 kda 2, ubch5b. Engineered: yes. Other_details: residue a 85 has been modified from cysteine by 2-mercaptoethanol to form s, s-(2-hydroxyethyl)thiocysteine.
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: rosetta.
Resolution:
1.94Å     R-factor:   0.227     R-free:   0.259
Authors: R.B.Dodd,R.J.Read
Key ref: R.B.Dodd and r.j.read Structures of two human ubiquitin-Conjugating enzymes from twinned crystals. To be published, .
Date:
21-Oct-05     Release date:   22-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P62837  (UB2D2_HUMAN) -  Ubiquitin-conjugating enzyme E2 D2
Seq:
Struc:
147 a.a.
150 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.19  - Ubiquitin--protein ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
ATP
+ ubiquitin
+ protein lysine
= AMP
+ diphosphate
+ protein N-ubiquityllysine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   4 terms 
  Biological process     TRIF-dependent toll-like receptor signaling pathway   13 terms 
  Biochemical function     nucleotide binding     6 terms