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PDBsum entry 5e2g

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
5e2g

 

 

 

 

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Contents
Protein chains
349 a.a.
Ligands
SCN ×6
ACY ×2
Waters ×702
PDB id:
5e2g
Name: Hydrolase
Title: Crystal structure of d-alanine carboxypeptidase ampc from burkholderia cenocepacia
Structure: Beta-lactamase. Chain: a, b. Fragment: residues 31-388. Engineered: yes
Source: Burkholderia cenocepacia. Organism_taxid: 216591. Strain: atcc baa-245 / dsm 16553 / lmg 16656 / nctc 13227 / j2315 / cf5610. Gene: ampc, bcas0156. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.65Å     R-factor:   0.153     R-free:   0.189
Authors: Y.Kim,G.Joachimiak,M.Endres,G.Babnigg,A.Joachimiak,Midwest Center For Structural Genomics (Mcsg)
Key ref: Y.Kim et al. Crystal structure of d-Alanine carboxypeptidase ampc burkholderia cenocepacia. To be published, .
Date:
01-Oct-15     Release date:   14-Oct-15    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
B4EPS2  (B4EPS2_BURCJ) -  Beta-lactamase from Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Seq:
Struc:
389 a.a.
349 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.5.2.6  - beta-lactamase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Penicillin Biosynthesis and Metabolism
      Reaction: a beta-lactam + H2O = a substituted beta-amino acid
      Cofactor: Zn(2+)

 

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