spacer
spacer

PDBsum entry 1e51

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Lyase PDB id
1e51
Jmol
Contents
Protein chains
326 a.a. *
299 a.a. *
Ligands
PBG
SO4 ×2
Metals
_ZN
* Residue conservation analysis
PDB id:
1e51
Name: Lyase
Title: Crystal structure of native human erythrocyte 5-aminolaevulinic acid dehydratase
Structure: Delta-aminolevulinic acid dehydratase. Chain: a, b. Synonym: aladh, porphobilinogen synthase, porphobilinogen s aladh. Other_details: porphobilinogen in active site of monomer a
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell: erythrocytes
Biol. unit: Octamer (from PDB file)
Resolution:
2.83Å     R-factor:   0.213     R-free:   0.270
Authors: N.L.Mills-Davies,D.Thompson,J.B.Cooper, P.M.Shoolingin-Jorda
Key ref: N.L.Mills-Davies et al. The crystal structure of human ala-Dehydratase. To be published, .
Date:
13-Jul-00     Release date:   12-Jul-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P13716  (HEM2_HUMAN) -  Delta-aminolevulinic acid dehydratase
Seq:
Struc:
330 a.a.
326 a.a.
Protein chain
Pfam   ArchSchema ?
P13716  (HEM2_HUMAN) -  Delta-aminolevulinic acid dehydratase
Seq:
Struc:
330 a.a.
299 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: 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
Bound ligand (Het Group name = PBG)
corresponds exactly
+ 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   3 terms 
  Biological process     metabolic process   9 terms 
  Biochemical function     catalytic activity     7 terms