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PDBsum entry 2z1b

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protein Protein-protein interface(s) links
Lyase PDB id
2z1b
Jmol
Contents
Protein chains
290 a.a. *
320 a.a. *
Waters ×57
* Residue conservation analysis
PDB id:
2z1b
Name: Lyase
Title: Crystal structure of 5-aminolevulinic acid dehydratase (alad) from mus musculs
Structure: Delta-aminolevulinic acid dehydratase. Chain: a, b, c, d. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: alad. Other_details: cell-free protein synthesis
Resolution:
3.30Å     R-factor:   0.278     R-free:   0.353
Authors: Y.Xie,H.Wang,M.Kawazoe,S.Kishishita,K.Murayama,C.Takemoto, T.Terada,M.Shirozu,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: Y.Xie et al. Crystal structure of 5-Aminolevulinic acid dehydratase (alad) from mus musculs. To be published, .
Date:
08-May-07     Release date:   13-May-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P10518  (HEM2_MOUSE) -  Delta-aminolevulinic acid dehydratase
Seq:
Struc:
330 a.a.
290 a.a.*
Protein chain
Pfam   ArchSchema ?
P10518  (HEM2_MOUSE) -  Delta-aminolevulinic acid dehydratase
Seq:
Struc:
330 a.a.
320 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D: E.C.4.2.1.24  - Porphobilinogen synthase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Porphyrin Biosynthesis (early stages)
      Reaction: 2 5-aminolevulinate = porphobilinogen + 2 H2O
2 × 5-aminolevulinate
= porphobilinogen
+ 2 × H(2)O
      Cofactor: Zn(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular vesicular exosome   2 terms 
  Biological process     metabolic process   7 terms 
  Biochemical function     catalytic activity     7 terms