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PDBsum entry 3rbf

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protein ligands metals Protein-protein interface(s) links
Lyase PDB id
3rbf
Jmol
Contents
Protein chains
443 a.a.
Ligands
PLP
Metals
_CL ×2
PDB id:
3rbf
Name: Lyase
Title: Crystal structure of human aromatic l-amino acid decarboxyla in the apo form
Structure: Aromatic-l-amino-acid decarboxylase. Chain: a, b. Synonym: aadc, dopa decarboxylase, ddc. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: aadc, ddc, hcg_1811384, tcag7.584. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.90Å     R-factor:   0.215     R-free:   0.267
Authors: G.Giardina,R.Montioli,S.Gianni,B.Cellini,A.Paiardini,C.Borri Voltattorni,F.Cutruzzola
Key ref: G.Giardina et al. (2011). Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. Proc Natl Acad Sci U S A, 108, 20514-20519. PubMed id: 22143761 DOI: 10.1073/pnas.1111456108
Date:
29-Mar-11     Release date:   19-Oct-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P20711  (DDC_HUMAN) -  Aromatic-L-amino-acid decarboxylase
Seq:
Struc:
480 a.a.
443 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.4.1.1.28  - Aromatic-L-amino-acid decarboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Dopa Biosynthesis
      Reaction:
1. L-dopa = dopamine + CO2
2. 5-hydroxy-L-tryptophan = 5-hydroxytryptamine + CO2
L-dopa
= dopamine
+ CO(2)
5-hydroxy-L-tryptophan
= 5-hydroxytryptamine
+ CO(2)
      Cofactor: Pyridoxal 5'-phosphate
Pyridoxal 5'-phosphate
Bound ligand (Het Group name = PLP) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     neuronal cell body   6 terms 
  Biological process     cellular response to drug   18 terms 
  Biochemical function     catalytic activity     8 terms  

 

 
    reference    
 
 
DOI no: 10.1073/pnas.1111456108 Proc Natl Acad Sci U S A 108:20514-20519 (2011)
PubMed id: 22143761  
 
 
Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases.
G.Giardina, R.Montioli, S.Gianni, B.Cellini, A.Paiardini, C.B.Voltattorni, F.Cutruzzolà.
 
  ABSTRACT  
 
No abstract given.