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PDBsum entry 3lmx

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3lmx
Jmol
Contents
Protein chains
200 a.a. *
238 a.a. *
Ligands
GOL ×10
SO4 ×11
BME ×23
DHB ×6
Metals
_CL ×6
_FE ×3
Waters ×600
* Residue conservation analysis
PDB id:
3lmx
Name: Oxidoreductase
Title: Tyrosine 447 of protocatechuate 34,-dioxygenase controls eff progress through catalysis
Structure: Protocatechuate 3,4-dioxygenase alpha chain. Chain: a, b, c. Synonym: 3,4-pcd. Engineered: yes. Protocatechuate 3,4-dioxygenase beta chain. Chain: m, n, o. Synonym: 3,4-pcd. Engineered: yes. Mutation: yes
Source: Pseudomonas putida. Organism_taxid: 303. Gene: pcag. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: pcah.
Resolution:
2.20Å     R-factor:   0.171     R-free:   0.213
Authors: V.M.Purpero,J.D.Lipscomb,K.Shi
Key ref: V.M.Purpero et al. Tyrosine 447 of protocatechuate 34,-Dioxygenase contr efficient progress through catalysis. To be published, .
Date:
01-Feb-10     Release date:   16-Feb-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00436  (PCXA_PSEPU) -  Protocatechuate 3,4-dioxygenase alpha chain
Seq:
Struc:
201 a.a.
200 a.a.
Protein chains
Pfam   ArchSchema ?
P00437  (PCXB_PSEPU) -  Protocatechuate 3,4-dioxygenase beta chain
Seq:
Struc:
239 a.a.
238 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chains A, M, B, N, C, O: E.C.1.13.11.3  - Protocatechuate 3,4-dioxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Benzoate Metabolism
      Reaction: 3,4-dihydroxybenzoate + O2 = 3-carboxy-cis,cis-muconate
3,4-dihydroxybenzoate
Bound ligand (Het Group name = DHB)
corresponds exactly
+ O(2)
= 3-carboxy-cis,cis-muconate
      Cofactor: Iron
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   5 terms 
  Biochemical function     catalytic activity     8 terms