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PDBsum entry 4dz4

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
4dz4
Jmol
Contents
Protein chains
(+ 0 more) 313 a.a.
Ligands
EDO ×47
UNK ×14
Metals
_MN ×12
Waters ×1784
PDB id:
4dz4
Name: Hydrolase
Title: X-ray crystal structure of a hypothetical agmatinase from bu thailandensis
Structure: Agmatinase. Chain: a, b, c, d, e, f. Engineered: yes
Source: Burkholderia thailandensis. Organism_taxid: 271848. Strain: e264 / atcc 700388 / dsm 13276 / cip 106301. Gene: bth_ii1941. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.154     R-free:   0.175
Authors: Seattle Structural Genomics Center For Infectious Disease (S
Key ref: L.Baugh et al. (2013). Combining functional and structural genomics to sample the essential Burkholderia structome. PLoS One, 8, e53851. PubMed id: 23382856
Date:
29-Feb-12     Release date:   28-Mar-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q2T3W4  (Q2T3W4_BURTA) -  Agmatinase, putative
Seq:
Struc:
320 a.a.
313 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.5.3.11  - Agmatinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Agmatine + H2O = putrescine + urea
Agmatine
+ H(2)O
= putrescine
+ urea
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   1 term 
  Biochemical function     hydrolase activity     4 terms  

 

 
    reference    
 
 
PLoS One 8:e53851 (2013)
PubMed id: 23382856  
 
 
Combining functional and structural genomics to sample the essential Burkholderia structome.
L.Baugh, L.A.Gallagher, R.Patrapuvich, M.C.Clifton, A.S.Gardberg, T.E.Edwards, B.Armour, D.W.Begley, S.H.Dieterich, D.M.Dranow, J.Abendroth, J.W.Fairman, D.Fox, B.L.Staker, I.Phan, A.Gillespie, R.Choi, S.Nakazawa-Hewitt, M.T.Nguyen, A.Napuli, L.Barrett, G.W.Buchko, R.Stacy, P.J.Myler, L.J.Stewart, C.Manoil, W.C.Van Voorhis.
 
  ABSTRACT  
 
No abstract given.